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Conserved domains on  [gi|2223346070|ref|WP_244935455|]
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ATP-binding protein [Pseudomonas sessilinigenes]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09959 super family cl32441
acid-sensing system histidine kinase EvgS;
16-971 6.18e-85

acid-sensing system histidine kinase EvgS;


The actual alignment was detected with superfamily member PRK09959:

Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 298.19  E-value: 6.18e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   16 RLEGLLADYVVALQRELGVPIRLRSFLTRDAMYAALRGGDLDMVSN-------INPLMAASHGLVLSPPYVLTELAlfse 88
Cdd:PRK09959    78 RVRGINADYLNLLKRALNIKLTLREYADHQKAMDALEEGEVDIVLShlvasppLNDDIAATKPLIITFPALVTTLH---- 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   89 ggDLHEYSIDDGQTRIA-VANGMMLELFRSAGGRGRFQHYPSALLAMASVLTGENEVFLGDALSTRYLSSQLFSNQLVVN 167
Cdd:PRK09959   154 --DSMRPLTSSKPVNIArVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGQNDYFIGSNIITSSMISRYFTHSLNVV 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  168 QSVKLPEVKVGFGLKPGNAILEGILKRALGGMTRCQKIRAQHLWGDNEVCSTSDFRSRLDAQELDWLDRAGTVRLAVSED 247
Cdd:PRK09959   232 KYYNSPRQYNFFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWLDTGNLAFLNKPLELTEHEKQWIKQHPDLKVLENPY 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  248 LAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVSSLSQANELLDHGAasLSILP---ETSPVELPYPHSDPLATAP 324
Cdd:PRK09959   312 SPPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLNPGG--WDIIPgaiYSEDRENNVLFAEAFITTP 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  325 YLFIQRQ--EAQETLDAQTRatVIIAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLVLAPANVARYYLSYKY 402
Cdd:PRK09959   390 YVFVMQKapDSEQTLKKGMK--VAIPYYYELHSQLKEMYPEVEWIKVDNASAAFHKVKEGELDALVATQLNSRYMIDHYY 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  403 ESSLKVGGIFDGPGVRIVFAAPHDQAQLISILDKAMLEITPRESLLIVGRW--RANSATD--DKYWEGV----------- 467
Cdd:PRK09959   468 PNELYHFLIPGVPNASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWikMPNVTIDtwDLYSEQFyivttlsvllv 547
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  468 -ASFIWRSFGLLGV--------------------------------------------------------MLLVAGM--- 487
Cdd:PRK09959   548 gSSLLWGFYLLRSVrrrkviqgdlenqisfrkalsdslpnptyvvnwqgnvishnsafehyftadyyknaMLPLENSdsp 627
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  488 ---------------------------------------------LIVAQRRRIRRKRQDLQQRQLLMDELQVAKESADH 522
Cdd:PRK09959   628 fkdvfsnahevtaetkenrtiytqvfeidngiekrcinhwhtlcnLPASDHAVYICGWQDITETRDLIHALEVERNKAIN 707
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  523 ASRAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLELAPEPAR 602
Cdd:PRK09959   708 ATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVD 787
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  603 MTVLLESVGNVFSGLARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVDLRCSVEAAGDSALSFRV 682
Cdd:PRK09959   788 IPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKM 867
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  683 SVTDTGAGIAAAQLGQVFQPFyvVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFVVVLERVMADCAT 762
Cdd:PRK09959   868 TIMDSGSGLSQEEQQQLFKRY--SQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVATV 945
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  763 LPEGEAPKShINEPLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTI 842
Cdd:PRK09959   946 EAKAEQPIT-LPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKL 1024
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  843 RrleQQQGGKPclIIGLTADAQREALQLCRDAGMDHALAKPTNLATLNRFIPKLGPDQSWASQ---------GLSWTNDI 913
Cdd:PRK09959  1025 R---EQNSSLP--IWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQyrhldiealKNNTANDL 1099
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2223346070  914 RasMARQVVASNQEES----AALRRALEEGDLPGAGRIAHKLKGTAYLLNHQALLEQCVEVE 971
Cdd:PRK09959  1100 Q--LMQEILMTFQHEThkdlPAAFHALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLE 1159
 
Name Accession Description Interval E-value
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
16-971 6.18e-85

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 298.19  E-value: 6.18e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   16 RLEGLLADYVVALQRELGVPIRLRSFLTRDAMYAALRGGDLDMVSN-------INPLMAASHGLVLSPPYVLTELAlfse 88
Cdd:PRK09959    78 RVRGINADYLNLLKRALNIKLTLREYADHQKAMDALEEGEVDIVLShlvasppLNDDIAATKPLIITFPALVTTLH---- 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   89 ggDLHEYSIDDGQTRIA-VANGMMLELFRSAGGRGRFQHYPSALLAMASVLTGENEVFLGDALSTRYLSSQLFSNQLVVN 167
Cdd:PRK09959   154 --DSMRPLTSSKPVNIArVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGQNDYFIGSNIITSSMISRYFTHSLNVV 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  168 QSVKLPEVKVGFGLKPGNAILEGILKRALGGMTRCQKIRAQHLWGDNEVCSTSDFRSRLDAQELDWLDRAGTVRLAVSED 247
Cdd:PRK09959   232 KYYNSPRQYNFFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWLDTGNLAFLNKPLELTEHEKQWIKQHPDLKVLENPY 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  248 LAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVSSLSQANELLDHGAasLSILP---ETSPVELPYPHSDPLATAP 324
Cdd:PRK09959   312 SPPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLNPGG--WDIIPgaiYSEDRENNVLFAEAFITTP 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  325 YLFIQRQ--EAQETLDAQTRatVIIAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLVLAPANVARYYLSYKY 402
Cdd:PRK09959   390 YVFVMQKapDSEQTLKKGMK--VAIPYYYELHSQLKEMYPEVEWIKVDNASAAFHKVKEGELDALVATQLNSRYMIDHYY 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  403 ESSLKVGGIFDGPGVRIVFAAPHDQAQLISILDKAMLEITPRESLLIVGRW--RANSATD--DKYWEGV----------- 467
Cdd:PRK09959   468 PNELYHFLIPGVPNASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWikMPNVTIDtwDLYSEQFyivttlsvllv 547
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  468 -ASFIWRSFGLLGV--------------------------------------------------------MLLVAGM--- 487
Cdd:PRK09959   548 gSSLLWGFYLLRSVrrrkviqgdlenqisfrkalsdslpnptyvvnwqgnvishnsafehyftadyyknaMLPLENSdsp 627
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  488 ---------------------------------------------LIVAQRRRIRRKRQDLQQRQLLMDELQVAKESADH 522
Cdd:PRK09959   628 fkdvfsnahevtaetkenrtiytqvfeidngiekrcinhwhtlcnLPASDHAVYICGWQDITETRDLIHALEVERNKAIN 707
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  523 ASRAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLELAPEPAR 602
Cdd:PRK09959   708 ATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVD 787
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  603 MTVLLESVGNVFSGLARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVDLRCSVEAAGDSALSFRV 682
Cdd:PRK09959   788 IPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKM 867
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  683 SVTDTGAGIAAAQLGQVFQPFyvVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFVVVLERVMADCAT 762
Cdd:PRK09959   868 TIMDSGSGLSQEEQQQLFKRY--SQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVATV 945
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  763 LPEGEAPKShINEPLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTI 842
Cdd:PRK09959   946 EAKAEQPIT-LPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKL 1024
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  843 RrleQQQGGKPclIIGLTADAQREALQLCRDAGMDHALAKPTNLATLNRFIPKLGPDQSWASQ---------GLSWTNDI 913
Cdd:PRK09959  1025 R---EQNSSLP--IWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQyrhldiealKNNTANDL 1099
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2223346070  914 RasMARQVVASNQEES----AALRRALEEGDLPGAGRIAHKLKGTAYLLNHQALLEQCVEVE 971
Cdd:PRK09959  1100 Q--LMQEILMTFQHEThkdlPAAFHALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLE 1159
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
516-971 1.26e-76

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 271.27  E-value: 1.26e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  516 AKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELvLTRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLE 595
Cdd:TIGR02956  453 ARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLEL-LGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLS 531
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  596 LAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVDLRCSVeaAGD 675
Cdd:TIGR02956  532 ISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL--NDD 609
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  676 SALSFrvSVTDTGAGIAAAQLGQVFQPFYVVDGAvgDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFVVVLER 755
Cdd:TIGR02956  610 SSLLF--EVEDTGCGIAEEEQATLFDAFTQADGR--RRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTR 685
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  756 vmADCATLPEGEAPKShINePLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGG 835
Cdd:TIGR02956  686 --GKPAEDSATLTVID-LP-PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDG 761
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  836 LEMARTIRRLEQQQGGKPclIIGLTADAQREALQLCRDAGMDHALAKPTNLATLNRFI---------------------- 893
Cdd:TIGR02956  762 VTLLQQLRAIYGAKNEVK--FIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIavilaggksnteapvlsaspsf 839
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  894 ------PKLGPDQSWASQGLSWT--------NDIR---ASMARQVVA----SNQEESAALRRALEEGDLPGAGRIAHKLK 952
Cdd:TIGR02956  840 dsasviENAQADDIPESNQASEFlldeeqlqQDIEvlgVEKVRQLVAlfktSSAEQLEELSAARAVDDDAQIKKLAHKLK 919
                          490
                   ....*....|....*....
gi 2223346070  953 GTAYLLNHQALLEQCVEVE 971
Cdd:TIGR02956  920 GSAGSLGLTQLTQLCQQLE 938
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
419-753 5.11e-67

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 227.87  E-value: 5.11e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  419 IVFAAPHDQAQLISILDKAMLEITPRESLLIVGRWRANSATDDKYWEGVASFIWRSFGLLGVMLLVAGMLIVAQRRRIRR 498
Cdd:COG0642      2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  499 KRQDLQQRQLLMDELQVAKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVltRRGETELDHQSMHIAYESAVSLLA 578
Cdd:COG0642     82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELL--LEELDEEQREYLETILRSADRLLR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  579 LIGDILDISRIESGKLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDAlASAQVWVDAVKVKQIVSNLLSNAIKF 658
Cdd:COG0642    160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPD-DLPTVRGDPDRLRQVLLNLLSNAIKY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  659 TEQGGVdLRCSVEAAGDSAlsfRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPnaGAGLGLAISQALCLLMGGTLEVK 738
Cdd:COG0642    239 TPEGGT-VTVSVRREGDRV---RISVEDTGPGIPPEDLERIFEPFFRTDPSRRGG--GTGLGLAIVKRIVELHGGTIEVE 312
                          330
                   ....*....|....*
gi 2223346070  739 SEEGTGTCmsFVVVL 753
Cdd:COG0642    313 SEPGKGTT--FTVTL 325
PBP2_BvgS_D1 cd13705
The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
6-212 7.42e-54

The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the first domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a histidine-kinase (HK), a receiver and a histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270423 [Multi-domain]  Cd Length: 221  Bit Score: 187.03  E-value: 7.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070    6 PPLRIFVEGPRLEGLLADYVVALQRELGVPIRLRSFLTRDAMYAALRGGDLDMVSNINPLMAASHGLVLSPPYVLTELAL 85
Cdd:cd13705     14 PPFDITSSGGRYEGITADYLGLIADALGVRVEVRRYPDREAALEALRNGEIDLLGTANGSEAGDGGLLLSQPYLPDQPVL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   86 FSEGGDLHEYSIDDGQTRIAVANGMMLELF-RSAGGRGRFQHYPSALLAMASVLTGENEVFLGDALSTRYLSSQLFSNQL 164
Cdd:cd13705     94 VTRIGDSRQPPPDLAGKRVAVVPGYLPAEEiKQAYPDARIVLYPSPLQALAAVAFGQADYFLGDAISANYLISRNYLNNL 173
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2223346070  165 VVNQSVKLPEVKVGFGLKPGNAILEGILKRALGGMTRCQKIRAQHLWG 212
Cdd:cd13705    174 RIVRFAPLPSRGFGFAVRPDNTRLLRLLNRALAAIPDEQRDEILRRWS 221
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
640-754 6.17e-29

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 111.59  E-value: 6.17e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   640 DAVKVKQIVSNLLSNAIKFTEQGGvDLRCSVEAAGDSAlsfRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPnAGAGL 719
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGG-RITVTLERDGDHV---EITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKI-GGTGL 76
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 2223346070   720 GLAISQALCLLMGGTLEVKSEEGTGTCMSFVVVLE 754
Cdd:smart00387   77 GLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
640-755 1.61e-24

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 98.98  E-value: 1.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  640 DAVKVKQIVSNLLSNAIKFTEQGGvDLRCSVEAAGDsalsFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGdpnAGAGL 719
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAG-EITVTLSEGGE----LTLTVEDNGIGIPPEDLPRIFEPFSTADKRGG---GGTGL 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2223346070  720 GLAISQALCLLMGGTLEVKSEEGTGTCMSFVVVLER 755
Cdd:pfam02518   74 GLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
524-756 1.26e-22

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 102.80  E-value: 1.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  524 SRAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGE--------TELdhqsMHIAYESAVSLLAligDILDISRIESGKLE 595
Cdd:NF040691   268 SRLQQRFVSDVSHELRTPLTTIRMAADVIHDSRDDfdpatarsAEL----LHTELDRFESLLS---DLLEISRFDAGAAE 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  596 LAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDALAsAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVDLRCsveAAGD 675
Cdd:NF040691   341 LDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGTP-VVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTV---AQDD 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  676 SALSfrVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCmsFVVVLER 755
Cdd:NF040691   417 TAVA--VTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQ--FRLTLPR 492

                   .
gi 2223346070  756 V 756
Cdd:NF040691   493 V 493
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
518-735 4.42e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.59  E-value: 4.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  518 ESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVltRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLELA 597
Cdd:NF012163   231 STLEKNEQMRRDFMADISHELRTPLAVLRAELEAI--QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQ 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  598 PEPARMTVLLESVGNVFSglARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGvDLRCSveaAGDSA 677
Cdd:NF012163   309 KASVDLVPLLEVEGGAFR--ERFASAGLELEVSLPDSSLVFGDRDRLMQLFNNLLENSLRYTDSGG-SLHIS---ASQRP 382
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2223346070  678 LSFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTL 735
Cdd:NF012163   383 KEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTL 440
 
Name Accession Description Interval E-value
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
16-971 6.18e-85

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 298.19  E-value: 6.18e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   16 RLEGLLADYVVALQRELGVPIRLRSFLTRDAMYAALRGGDLDMVSN-------INPLMAASHGLVLSPPYVLTELAlfse 88
Cdd:PRK09959    78 RVRGINADYLNLLKRALNIKLTLREYADHQKAMDALEEGEVDIVLShlvasppLNDDIAATKPLIITFPALVTTLH---- 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   89 ggDLHEYSIDDGQTRIA-VANGMMLELFRSAGGRGRFQHYPSALLAMASVLTGENEVFLGDALSTRYLSSQLFSNQLVVN 167
Cdd:PRK09959   154 --DSMRPLTSSKPVNIArVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGQNDYFIGSNIITSSMISRYFTHSLNVV 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  168 QSVKLPEVKVGFGLKPGNAILEGILKRALGGMTRCQKIRAQHLWGDNEVCSTSDFRSRLDAQELDWLDRAGTVRLAVSED 247
Cdd:PRK09959   232 KYYNSPRQYNFFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWLDTGNLAFLNKPLELTEHEKQWIKQHPDLKVLENPY 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  248 LAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVSSLSQANELLDHGAasLSILP---ETSPVELPYPHSDPLATAP 324
Cdd:PRK09959   312 SPPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLNPGG--WDIIPgaiYSEDRENNVLFAEAFITTP 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  325 YLFIQRQ--EAQETLDAQTRatVIIAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLVLAPANVARYYLSYKY 402
Cdd:PRK09959   390 YVFVMQKapDSEQTLKKGMK--VAIPYYYELHSQLKEMYPEVEWIKVDNASAAFHKVKEGELDALVATQLNSRYMIDHYY 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  403 ESSLKVGGIFDGPGVRIVFAAPHDQAQLISILDKAMLEITPRESLLIVGRW--RANSATD--DKYWEGV----------- 467
Cdd:PRK09959   468 PNELYHFLIPGVPNASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWikMPNVTIDtwDLYSEQFyivttlsvllv 547
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  468 -ASFIWRSFGLLGV--------------------------------------------------------MLLVAGM--- 487
Cdd:PRK09959   548 gSSLLWGFYLLRSVrrrkviqgdlenqisfrkalsdslpnptyvvnwqgnvishnsafehyftadyyknaMLPLENSdsp 627
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  488 ---------------------------------------------LIVAQRRRIRRKRQDLQQRQLLMDELQVAKESADH 522
Cdd:PRK09959   628 fkdvfsnahevtaetkenrtiytqvfeidngiekrcinhwhtlcnLPASDHAVYICGWQDITETRDLIHALEVERNKAIN 707
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  523 ASRAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLELAPEPAR 602
Cdd:PRK09959   708 ATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVD 787
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  603 MTVLLESVGNVFSGLARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVDLRCSVEAAGDSALSFRV 682
Cdd:PRK09959   788 IPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKM 867
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  683 SVTDTGAGIAAAQLGQVFQPFyvVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFVVVLERVMADCAT 762
Cdd:PRK09959   868 TIMDSGSGLSQEEQQQLFKRY--SQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVATV 945
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  763 LPEGEAPKShINEPLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTI 842
Cdd:PRK09959   946 EAKAEQPIT-LPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKL 1024
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  843 RrleQQQGGKPclIIGLTADAQREALQLCRDAGMDHALAKPTNLATLNRFIPKLGPDQSWASQ---------GLSWTNDI 913
Cdd:PRK09959  1025 R---EQNSSLP--IWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQyrhldiealKNNTANDL 1099
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2223346070  914 RasMARQVVASNQEES----AALRRALEEGDLPGAGRIAHKLKGTAYLLNHQALLEQCVEVE 971
Cdd:PRK09959  1100 Q--LMQEILMTFQHEThkdlPAAFHALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLE 1159
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
516-971 1.26e-76

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 271.27  E-value: 1.26e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  516 AKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELvLTRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLE 595
Cdd:TIGR02956  453 ARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLEL-LGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLS 531
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  596 LAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVDLRCSVeaAGD 675
Cdd:TIGR02956  532 ISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL--NDD 609
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  676 SALSFrvSVTDTGAGIAAAQLGQVFQPFYVVDGAvgDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFVVVLER 755
Cdd:TIGR02956  610 SSLLF--EVEDTGCGIAEEEQATLFDAFTQADGR--RRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTR 685
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  756 vmADCATLPEGEAPKShINePLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGG 835
Cdd:TIGR02956  686 --GKPAEDSATLTVID-LP-PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDG 761
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  836 LEMARTIRRLEQQQGGKPclIIGLTADAQREALQLCRDAGMDHALAKPTNLATLNRFI---------------------- 893
Cdd:TIGR02956  762 VTLLQQLRAIYGAKNEVK--FIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIavilaggksnteapvlsaspsf 839
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  894 ------PKLGPDQSWASQGLSWT--------NDIR---ASMARQVVA----SNQEESAALRRALEEGDLPGAGRIAHKLK 952
Cdd:TIGR02956  840 dsasviENAQADDIPESNQASEFlldeeqlqQDIEvlgVEKVRQLVAlfktSSAEQLEELSAARAVDDDAQIKKLAHKLK 919
                          490
                   ....*....|....*....
gi 2223346070  953 GTAYLLNHQALLEQCVEVE 971
Cdd:TIGR02956  920 GSAGSLGLTQLTQLCQQLE 938
PRK15347 PRK15347
two component system sensor kinase;
512-990 1.45e-68

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 247.25  E-value: 1.45e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  512 ELQVAKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVLTrrgeTELDHQSMHI---AYESAVSLLALIGDILDISR 588
Cdd:PRK15347   383 ALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQN----TPLTAEQMDLadtARQCTLSLLAIINNLLDFSR 458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  589 IESGKLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVDLRC 668
Cdd:PRK15347   459 IESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRV 538
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  669 SVEaagDSALSFRVSvtDTGAGIAAAQLGQVFQPFYVVDgavgDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMS 748
Cdd:PRK15347   539 KRH---EQQLCFTVE--DTGCGIDIQQQQQIFTPFYQAD----THSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFS 609
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  749 FVVVLER-------------------------------------VMADCATLP-----------EGEAPKSHINEPLS-- 778
Cdd:PRK15347   610 LVLPLNEyappeplkgelsaplalhrqlsawgitcqpghqnpalLDPELAYLPgrlydllqqiiQGAPNEPVINLPLQpw 689
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 ---VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQGGKpCL 855
Cdd:PRK15347   690 qlqILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPD-CM 768
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  856 IIGLTADAQREALQLCRDAGMDHALAKPTNLATLNRFI----------------------PKLGPDQSWASQGLSWTNDI 913
Cdd:PRK15347   769 IVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALelaaeyqllrgielspqdsscsPLLDTDDMALNSKLYQSLLL 848
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  914 RASMARQVVAsNQEEsaaLRRALeegdlpgagriaHKLKGTA------YLLNHQALLEQCVEVEELCSGELTEEFGETVQ 987
Cdd:PRK15347   849 LLAQIEQAVE-NQEV---LSQLL------------HTLKGCAgqagltELQCAVIDLENALETGEILSLEELTDLRELIH 912

                   ...
gi 2223346070  988 ILL 990
Cdd:PRK15347   913 ALF 915
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
419-753 5.11e-67

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 227.87  E-value: 5.11e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  419 IVFAAPHDQAQLISILDKAMLEITPRESLLIVGRWRANSATDDKYWEGVASFIWRSFGLLGVMLLVAGMLIVAQRRRIRR 498
Cdd:COG0642      2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  499 KRQDLQQRQLLMDELQVAKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVltRRGETELDHQSMHIAYESAVSLLA 578
Cdd:COG0642     82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELL--LEELDEEQREYLETILRSADRLLR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  579 LIGDILDISRIESGKLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDAlASAQVWVDAVKVKQIVSNLLSNAIKF 658
Cdd:COG0642    160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPD-DLPTVRGDPDRLRQVLLNLLSNAIKY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  659 TEQGGVdLRCSVEAAGDSAlsfRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPnaGAGLGLAISQALCLLMGGTLEVK 738
Cdd:COG0642    239 TPEGGT-VTVSVRREGDRV---RISVEDTGPGIPPEDLERIFEPFFRTDPSRRGG--GTGLGLAIVKRIVELHGGTIEVE 312
                          330
                   ....*....|....*
gi 2223346070  739 SEEGTGTCmsFVVVL 753
Cdd:COG0642    313 SEPGKGTT--FTVTL 325
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
516-896 2.67e-65

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 235.61  E-value: 2.67e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  516 AKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVLtrrgETELD---HQSMHIAYESAVSLLALIGDILDISRIESG 592
Cdd:PRK11091   272 YQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILL----DTELTaeqRKYLKTIHVSAITLGNIFNDIIDMDKMERR 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  593 KLELAPEPARMTVLLESVGNvFSGL-ARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVDLRCSVE 671
Cdd:PRK11091   348 KLQLDNQPIDFTDFLADLEN-LSGLqAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYE 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  672 AAGDsaLSFRVSvtDTGAGIAAAQLGQVFQPFY-VVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFV 750
Cdd:PRK11091   427 EGDM--LTFEVE--DSGIGIPEDELDKIFAMYYqVKDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLT 502
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  751 VVLERVMADcatLPEGEAPKSHINEPLSVLVVED----HLPSQYLLVQqvgyLGHRVLAASNGLEGLATWSEHAVDIVIS 826
Cdd:PRK11091   503 IHAPAVAEE---VEDAFDEDDMPLPALNILLVEDielnVIVARSVLEK----LGNSVDVAMTGKEALEMFDPDEYDLVLL 575
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2223346070  827 DCNMPQMGGLEMARTIRRLEQQQGGKPclIIGLTAD---AQREALqlcrDAGMDHALAKPTNLATLNRFIPKL 896
Cdd:PRK11091   576 DIQLPDMTGLDIARELRERYPREDLPP--LVALTANvlkDKKEYL----DAGMDDVLSKPLSVPALTAMIKKF 642
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
512-753 7.51e-63

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 213.23  E-value: 7.51e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  512 ELQVAKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGETELDHQSM-HIAYESAVSLLALIGDILDISRIE 590
Cdd:COG2205      1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPEERRELlEIIRESAERLLRLIEDLLDLSRLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  591 SGKLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDAlASAQVWVDAVKVKQIVSNLLSNAIKFTEQGG-VDLRCS 669
Cdd:COG2205     81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPP-ELPLVYADPELLEQVLANLLDNAIKYSPPGGtITISAR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  670 VEAAGdsalsFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPnaGAGLGLAISQALCLLMGGTLEVKSEEGTGTCmsF 749
Cdd:COG2205    160 REGDG-----VRISVSDNGPGIPEEELERIFERFYRGDNSRGEG--GTGLGLAIVKRIVEAHGGTIWVESEPGGGTT--F 230

                   ....
gi 2223346070  750 VVVL 753
Cdd:COG2205    231 TVTL 234
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
426-750 2.28e-60

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 211.72  E-value: 2.28e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  426 DQAQLISILDKAMLEITPRESLLIVGRWRANSATDDKYWEGVASFIWRSFGLLGVMLLVAGMLIVAQRRRIRRKRQDLQQ 505
Cdd:COG5002     64 LLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLL 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  506 RQLLMDELQVAKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGET-ELDHQSMHIAYESAVSLLALIGDIL 584
Cdd:COG5002    144 GLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDpEERREYLEIILEEAERLSRLVNDLL 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  585 DISRIESGKLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDAlASAQVWVDAVKVKQIVSNLLSNAIKFTEQGG- 663
Cdd:COG5002    224 DLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPE-DPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGt 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  664 VDLRCSVEAAGdsalsFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGT 743
Cdd:COG5002    303 ITVSLREEDDQ-----VRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGK 377

                   ....*..
gi 2223346070  744 GTCMSFV 750
Cdd:COG5002    378 GTTFTIT 384
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
510-889 3.43e-60

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 222.54  E-value: 3.43e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  510 MDE-LQVAKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGETELDH--QSMHiayESAVSLLALIGDILDI 586
Cdd:PRK10841   429 MEEsLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRlvTAMN---NSSSLLLKIISDILDF 505
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  587 SRIESGKLELAP-EPARMTVLLESVGNVFSgLARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVD 665
Cdd:PRK10841   506 SKIESEQLKIEPrEFSPREVINHITANYLP-LVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIV 584
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  666 LRCSVEaagDSALSFRVSvtDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGT 745
Cdd:PRK10841   585 LHVRVD---GDYLSFRVR--DTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGS 659
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  746 cmSFVV----------------------------------VLERVMADC---ATLPEGEAP------------------- 769
Cdd:PRK10841   660 --QFTIriplygaqypqkkgveglqgkrcwlavrnasleqFLETLLQRSgiqVQRYEGQEPtpedvlitddpvqkkwqgr 737
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  770 ------KSHI---------------------------------------------------NEPLSVLVVEDHLPSQYLL 792
Cdd:PRK10841   738 avitfcRRHIgipleiapgewvhstatphelpallariyrielesddsanalpstdkavsdNDDMMILVVDDHPINRRLL 817
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  793 VQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLeqqqgGKPCLIIGLTADAQREALQLCR 872
Cdd:PRK10841   818 ADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQL-----GLTLPVIGVTANALAEEKQRCL 892
                          490
                   ....*....|....*..
gi 2223346070  873 DAGMDHALAKPTNLATL 889
Cdd:PRK10841   893 EAGMDSCLSKPVTLDVL 909
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
512-889 1.94e-57

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 214.33  E-value: 1.94e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  512 ELQVAKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVL-TRRGETELDHqsMHIAYESAVSLLALIGDILDISRIE 590
Cdd:PRK11107   278 ELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLkTPLTPTQRDY--LQTIERSANNLLAIINDILDFSKLE 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  591 SGKLELA--PEPARMTvlLESVGNVFSGLARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVDLRC 668
Cdd:PRK11107   356 AGKLVLEniPFSLRET--LDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILV 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  669 SVEAAGDSALSFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMS 748
Cdd:PRK11107   434 ELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFW 513
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  749 FVVVLErvmadcatLPEGEAPKSHINEPL---SVLVVEDHLPSQYLLVQQvgyLGHRVLAASNGLEgLATWSEHAVDIVI 825
Cdd:PRK11107   514 FHLPLD--------LNPNPIIDGLPTDCLagkRLLYVEPNSAAAQATLDI---LSETPLEVTYSPT-LSQLPEAHYDILL 581
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2223346070  826 sdCNMPQMGGLEMARTIRRLEQQQGGKPCLIIGLTADAQREALQLCRDaGMDHALAKPTNLATL 889
Cdd:PRK11107   582 --LGLPVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLKQD-GADACLSKPLSHTRL 642
PBP2_BvgS_D1 cd13705
The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
6-212 7.42e-54

The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the first domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a histidine-kinase (HK), a receiver and a histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270423 [Multi-domain]  Cd Length: 221  Bit Score: 187.03  E-value: 7.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070    6 PPLRIFVEGPRLEGLLADYVVALQRELGVPIRLRSFLTRDAMYAALRGGDLDMVSNINPLMAASHGLVLSPPYVLTELAL 85
Cdd:cd13705     14 PPFDITSSGGRYEGITADYLGLIADALGVRVEVRRYPDREAALEALRNGEIDLLGTANGSEAGDGGLLLSQPYLPDQPVL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   86 FSEGGDLHEYSIDDGQTRIAVANGMMLELF-RSAGGRGRFQHYPSALLAMASVLTGENEVFLGDALSTRYLSSQLFSNQL 164
Cdd:cd13705     94 VTRIGDSRQPPPDLAGKRVAVVPGYLPAEEiKQAYPDARIVLYPSPLQALAAVAFGQADYFLGDAISANYLISRNYLNNL 173
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2223346070  165 VVNQSVKLPEVKVGFGLKPGNAILEGILKRALGGMTRCQKIRAQHLWG 212
Cdd:cd13705    174 RIVRFAPLPSRGFGFAVRPDNTRLLRLLNRALAAIPDEQRDEILRRWS 221
PBP2_BvgS_D2 cd13707
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
239-454 2.26e-51

The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270425 [Multi-domain]  Cd Length: 221  Bit Score: 180.11  E-value: 2.26e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  239 TVRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVSSLSQANELLDHGAASLSI-LPETSPVELPYPHS 317
Cdd:cd13707      3 VVRVVVNPDLAPLSFFDSNGQFRGISADLLELISLRTGLRFEVVRASSPAEMIEALRSGEADMIAaLTPSPEREDFLLFT 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  318 DPLATAPYLFIQRQ--EAQETLDAQTRATVIIAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLVLAPANVAR 395
Cdd:cd13707     83 RPYLTSPFVLVTRKdaAAPSSLEDLAGKRVAIPAGSALEDLLRRRYPQIELVEVDNTAEALALVASGKADATVASLISAR 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2223346070  396 YYLSYKYESSLKVGGIFDGPGVRIVFAAPHDQAQLISILDKAMLEITPRESLLIVGRWR 454
Cdd:cd13707    163 YLINHYFRDRLKIAGILGEPPAPIAFAVRRDQPELLSILDKALLSIPPDELLELRNRWR 221
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
507-971 5.72e-48

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 185.49  E-value: 5.72e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  507 QLLMDELQVAKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELvLTRRGETELDHQSMHIAYESAVSLLALIGDILDI 586
Cdd:PRK11466   424 QELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQL-LADNPALNAQRDDLRAITDSGESLLTILNDILDY 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  587 SRIESG--KLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGV 664
Cdd:PRK11466   503 SAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSI 582
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  665 DLRCSVEAAgdsalSFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGdpnaGAGLGLAISQALCLLMGGTLEVKSEEGTG 744
Cdd:PRK11466   583 VLRSRTDGE-----QWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRG----GTGLGLTISSRLAQAMGGELSATSTPEVG 653
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  745 TCMSFVVVLERvmadcATLPEGEAPKSHIN-EPLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSE-HAVD 822
Cdd:PRK11466   654 SCFCLRLPLRV-----ATAPVPKTVNQAVRlDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNsEPFA 728
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  823 IVISDCNMPQMGGLEMARTIRRLEQQqggkpCLIIGLTADAQREALQLcRDAGMDHAL-AKPTNLATLNRFIPKLGPDQS 901
Cdd:PRK11466   729 AALVDFDLPDYDGITLARQLAQQYPS-----LVLIGFSAHVIDETLRQ-RTSSLFRGIiPKPVPREVLGQLLAHYLQLQV 802
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  902 WASQGL--SWTNDIRASMA-----------RQVVASNQEESAALRRAleeGDLPGAGRIAHKLKGTAYLLNHQALLEQCV 968
Cdd:PRK11466   803 NNDQPLdvSQLNEDAALMGtekihewlalfKQHALPLLDEIDIARAS---QDSEKIKRAAHQLKSSCSSLGMRQASQACA 879

                   ...
gi 2223346070  969 EVE 971
Cdd:PRK11466   880 QLE 882
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
644-753 7.08e-38

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 137.24  E-value: 7.08e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  644 VKQIVSNLLSNAIKFTEQGGVDLRCSVEAAGDSALSFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAI 723
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2223346070  724 SQALCLLMGGTLEVKSEEGTGTCMSFVVVL 753
Cdd:cd16922     81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
779-889 1.18e-34

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 127.97  E-value: 1.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEqqQGGKPCLIIG 858
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELE--GGGRRTPIIA 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2223346070  859 LTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:cd17546     79 LTANALEEDREKCLEAGMDDYLSKPVKLDQL 109
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
238-453 1.82e-34

The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine kinase receptors, and related proteins; This family comprises the periplasmic sensor domain of the two-component sensor-kinase systems, such as the sensor protein BvgS of Bordetella pertussis and histidine kinase receptors (HisK), and uncharacterized related proteins. Typically, the two-component system consists of a membrane spanning sensor-kinase and a cytoplasmic response regulator. It serves as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. The N-terminal sensing domain of the sensor kinase detects extracellular signals, such as small molecule ligands and ions, which then modulate the catalytic activity of the cytoplasmic kinase domain through a phosphorylation cascade. The periplasmic sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270228 [Multi-domain]  Cd Length: 220  Bit Score: 131.50  E-value: 1.82e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  238 GTVRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVSSLSQANELLDHG----AASLSILPETSPVELP 313
Cdd:cd01007      2 PVIRVGVDPDWPPFEFIDEGGEPQGIAADYLKLIAKKLGLKFEYVPGDSWSELLEALKAGeidlLSSVSKTPEREKYLLF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  314 yphSDPLATAPYLFIQRQEAQ--ETLDAQTRATVIIAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLVLAPA 391
Cdd:cd01007     82 ---TKPYLSSPLVIVTRKDAPfiNSLSDLAGKRVAVVKGYALEELLRERYPNINLVEVDSTEEALEAVASGEADAYIGNL 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2223346070  392 NVARYYLSYKYESSLKVGGIFDGPgVRIVFAAPHDQAQLISILDKAMLEITPRESLLIVGRW 453
Cdd:cd01007    159 AVASYLIQKYGLSNLKIAGLTDYP-QDLSFAVRKDWPELLSILNKALASISPEERQAIRNKW 219
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
226-749 7.51e-33

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 134.14  E-value: 7.51e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  226 LDAQELDWLDRAGTVRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVSSLSQANELLDHGAASLSILP 305
Cdd:COG4251      1 LLLLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  306 ETSPVELPYPHSDPLATAPYLFIQRQEAQETLDAQTRATVIIAKGYVEPQQFRAQypylvfketqtmgEAFKQLRDGGAD 385
Cdd:COG4251     81 LLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALL-------------LLEELALLRLAL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  386 LVLAPANVARYYLSYKYESSLKVGGIFDGPGVRIVFAAPHDQAQLISILDKAMLEITPRESLLIVGRWRANSATDDKYWE 465
Cdd:COG4251    148 ALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGL 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  466 GVASFIWRSFGLLGVMLLVAGMLIVAQRRRIRRKRQDLQQRQLLMDELQVAKESADHasraksvFLATMSHEIRTPLNAI 545
Cdd:COG4251    228 LLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQ-------FAYVASHDLREPLRKI 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  546 IGMLELvLTRRGETELD---HQSMHIAYESAVSLLALIGDILDISRIesGKLELAPEPARMTVLLESVGNVFSGLARQKQ 622
Cdd:COG4251    301 SGFSQL-LEEDYGDKLDeegREYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERG 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  623 LRLTldIDALAsaQVWVDAVKVKQIVSNLLSNAIKFTEQGG---VDLRCSVEAAGdsalsFRVSVTDTGAGIAAAQLGQV 699
Cdd:COG4251    378 AEIE--VGPLP--TVRGDPTLLRQVFQNLISNAIKYSRPGEpprIEIGAEREGGE-----WVFSVRDNGIGIDPEYAEKI 448
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 2223346070  700 FQPFYVVDGAvgDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSF 749
Cdd:COG4251    449 FEIFQRLHSR--DEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYF 496
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
530-750 1.21e-32

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 129.64  E-value: 1.21e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  530 FLATMSHEIRTPLNAIIGMLELVL-TRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLELAPEPARMTVLLE 608
Cdd:TIGR02966  117 FVANVSHELRTPLTVLRGYLETLAdGPDEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLD 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  609 SVGNVFSGLARQKQLRLTLDIDalasAQVWV--DAVKVKQIVSNLLSNAIKFTEQGG-VDLRCSVEAAGdsalsFRVSVT 685
Cdd:TIGR02966  197 HLRDEAEALSQGKNHQITFEID----GGVDVlgDEDELRSAFSNLVSNAIKYTPEGGtITVRWRRDGGG-----AEFSVT 267
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2223346070  686 DTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFV 750
Cdd:TIGR02966  268 DTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFI 332
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
418-753 2.72e-32

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 129.53  E-value: 2.72e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  418 RIVFAAPHDQAQLISILDKAMLEITPRESLLIVGRWRANSATDDKYWEGVASFIWRSFGLLGVMLLVAGMLIVAQRRRIR 497
Cdd:COG4191     31 LLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEENAELE 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  498 RKRQDLQQRQLLMDELQVAKESADHASRAKSV--FLATMSHEIRTPLNAIIGMLELV---LTRRGETELDHQSMHIAYES 572
Cdd:COG4191    111 ELERDITELERAEEELRELQEQLVQSEKLAALgeLAAGIAHEINNPLAAILGNAELLrrrLEDEPDPEELREALERILEG 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  573 AVSLLALIGDILDISRiesgKLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDAlASAQVWVDAVKVKQIVSNLL 652
Cdd:COG4191    191 AERAAEIVRSLRAFSR----RDEEEREPVDLNELIDEALELLRPRLKARGIEVELDLPP-DLPPVLGDPGQLEQVLLNLL 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  653 SNAIK-FTEQGGVDLRCSVEAAGDSAlsfRVSVTDTGAGIAAAQLGQVFQPFYvvdgAVGDpnaGAGLGLAISQALCLLM 731
Cdd:COG4191    266 INAIDaMEEGEGGRITISTRREGDYV---VISVRDNGPGIPPEVLERIFEPFFtt-kPVGK---GTGLGLSISYGIVEKH 338
                          330       340
                   ....*....|....*....|..
gi 2223346070  732 GGTLEVKSEEGTGTCmsFVVVL 753
Cdd:COG4191    339 GGRIEVESEPGGGTT--FTITL 358
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
640-754 6.17e-29

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 111.59  E-value: 6.17e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   640 DAVKVKQIVSNLLSNAIKFTEQGGvDLRCSVEAAGDSAlsfRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPnAGAGL 719
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGG-RITVTLERDGDHV---EITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKI-GGTGL 76
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 2223346070   720 GLAISQALCLLMGGTLEVKSEEGTGTCMSFVVVLE 754
Cdd:smart00387   77 GLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
775-889 5.67e-27

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 106.86  E-value: 5.67e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  775 EPLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQGGKpc 854
Cdd:COG0784      4 GGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIP-- 81
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2223346070  855 lIIGLTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:COG0784     82 -IIALTAYADEEDRERALEAGADDYLTKPVDPEEL 115
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
532-753 2.19e-25

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 110.05  E-value: 2.19e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  532 ATMSHEIRTPLNAIIGMLELvLTRR------GETELDHQSMHIAYESAVSLLALIGDILDISRIEsgklELAPEPARMTV 605
Cdd:COG5000    206 RRIAHEIKNPLTPIQLSAER-LRRKladkleEDREDLERALDTIIRQVDRLKRIVDEFLDFARLP----EPQLEPVDLNE 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  606 LLESVGNVFSGLARQKQLRLTLDIDAlASAQVWVDAVKVKQIVSNLLSNAIKFTEQGG-VDLRCSVEAAgdsalSFRVSV 684
Cdd:COG5000    281 LLREVLALYEPALKEKDIRLELDLDP-DLPEVLADRDQLEQVLINLLKNAIEAIEEGGeIEVSTRREDG-----RVRIEV 354
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2223346070  685 TDTGAGIAAAQLGQVFQPFYvvdgavgdpNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCmsFVVVL 753
Cdd:COG5000    355 SDNGPGIPEEVLERIFEPFFtt------kPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTT--FTIRL 415
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
512-749 3.40e-25

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 110.45  E-value: 3.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  512 ELQVAKESADHASRAkSVFLATMSHEIRTPLNAIIGMLELVLtrrgETELDHQSMHiaYESAVS----LLALIGDILDIS 587
Cdd:COG5809    256 KLEELLRKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLK----DTIDEEQKTY--LDIMLSeldrIESIISEFLVLA 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  588 RIESGKLElapeparMTVLLESVGNVFSGLARQ-----KQLRLTLDIDAlasAQVWVDAVKVKQIVSNLLSNAIKFTEQG 662
Cdd:COG5809    329 KPQAIKYE-------PKDLNTLIEEVIPLLQPQallknVQIELELEDDI---PDILGDENQLKQVFINLLKNAIEAMPEG 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  663 GvDLRCSVEAAGDSALsfRVSVTDTGAGIAAAQLGQVFQPFYVVDgavgdpNAGAGLGLAISQALCLLMGGTLEVKSEEG 742
Cdd:COG5809    399 G-NITIETKAEDDDKV--VISVTDEGCGIPEERLKKLGEPFYTTK------EKGTGLGLMVSYKIIEEHGGKITVESEVG 469

                   ....*..
gi 2223346070  743 TGTCMSF 749
Cdd:COG5809    470 KGTTFSI 476
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
528-742 3.57e-25

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 110.17  E-value: 3.57e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  528 SVFLATMSHEIRTPLNAIIGMLELVLTRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLELAPEPARMTVLL 607
Cdd:TIGR01386  242 SQFSADLAHELRTPLTNLLGQTQVALSQPRTGEEYREVLESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAEL 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  608 ESVGNVFSGLARQKQLRLTLDidalASAQVWVDAVKVKQIVSNLLSNAIKFTEQGG-VDLRCsveaaGDSALSFRVSVTD 686
Cdd:TIGR01386  322 AKVAEYFEPLAEERGVRIRVE----GEGLVRGDPQMFRRAISNLLSNALRHTPDGGtITVRI-----ERRSDEVRVSVSN 392
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2223346070  687 TGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEG 742
Cdd:TIGR01386  393 PGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDG 448
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
501-753 1.33e-24

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 106.85  E-value: 1.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  501 QDLQQRQLLMDELQvakesadHASRAKSV--FLATMSHEIRTPLNAIIGMLELvLTRRGETELDHQSMHIAYESAVSLLA 578
Cdd:COG3852    114 RDITERKRLERELR-------RAEKLAAVgeLAAGLAHEIRNPLTGIRGAAQL-LERELPDDELREYTQLIIEEADRLNN 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  579 LIGDILDISRIESGKLElapePARMTVLLESVGNVF-SGLARQKQLRLTLDIDAlasAQVWVDAVKVKQIVSNLLSNAIK 657
Cdd:COG3852    186 LVDRLLSFSRPRPPERE----PVNLHEVLERVLELLrAEAPKNIRIVRDYDPSL---PEVLGDPDQLIQVLLNLVRNAAE 258
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  658 FTEQGGVdLRCSVEAAGDSALSF-------RVSVTDTGAGIAAAQLGQVFQPFYVvdgavGDPNaGAGLGLAISQALCLL 730
Cdd:COG3852    259 AMPEGGT-ITIRTRVERQVTLGGlrprlyvRIEVIDNGPGIPEEILDRIFEPFFT-----TKEK-GTGLGLAIVQKIVEQ 331
                          250       260
                   ....*....|....*....|...
gi 2223346070  731 MGGTLEVKSEEGTGTCmsFVVVL 753
Cdd:COG3852    332 HGGTIEVESEPGKGTT--FRIYL 352
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
640-755 1.61e-24

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 98.98  E-value: 1.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  640 DAVKVKQIVSNLLSNAIKFTEQGGvDLRCSVEAAGDsalsFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGdpnAGAGL 719
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAG-EITVTLSEGGE----LTLTVEDNGIGIPPEDLPRIFEPFSTADKRGG---GGTGL 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2223346070  720 GLAISQALCLLMGGTLEVKSEEGTGTCMSFVVVLER 755
Cdd:pfam02518   74 GLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
6-210 6.07e-23

The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine kinase receptors, and related proteins; This family comprises the periplasmic sensor domain of the two-component sensor-kinase systems, such as the sensor protein BvgS of Bordetella pertussis and histidine kinase receptors (HisK), and uncharacterized related proteins. Typically, the two-component system consists of a membrane spanning sensor-kinase and a cytoplasmic response regulator. It serves as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. The N-terminal sensing domain of the sensor kinase detects extracellular signals, such as small molecule ligands and ions, which then modulate the catalytic activity of the cytoplasmic kinase domain through a phosphorylation cascade. The periplasmic sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270228 [Multi-domain]  Cd Length: 220  Bit Score: 98.37  E-value: 6.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070    6 PPLRIFVEGPRLEGLLADYVVALQRELGVPIRLRSFLTRDAMYAALRGGDLDMVSNINPLMAASHGLVLSPPYVLTELAL 85
Cdd:cd01007     13 PPFEFIDEGGEPQGIAADYLKLIAKKLGLKFEYVPGDSWSELLEALKAGEIDLLSSVSKTPEREKYLLFTKPYLSSPLVI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   86 FSEGGDLHEYSIDD--GQtRIAVANG-MMLELFRSAGGRGRFQHYPSALLAMASVLTGENEVFLGDALSTRYLSSQLFSN 162
Cdd:cd01007     93 VTRKDAPFINSLSDlaGK-RVAVVKGyALEELLRERYPNINLVEVDSTEEALEAVASGEADAYIGNLAVASYLIQKYGLS 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2223346070  163 QLVVNQSVKLPEvKVGFGLKPGNAILEGILKRALGGMT--RCQKIRAQHL 210
Cdd:cd01007    172 NLKIAGLTDYPQ-DLSFAVRKDWPELLSILNKALASISpeERQAIRNKWL 220
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
524-756 1.26e-22

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 102.80  E-value: 1.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  524 SRAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGE--------TELdhqsMHIAYESAVSLLAligDILDISRIESGKLE 595
Cdd:NF040691   268 SRLQQRFVSDVSHELRTPLTTIRMAADVIHDSRDDfdpatarsAEL----LHTELDRFESLLS---DLLEISRFDAGAAE 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  596 LAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDALAsAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVDLRCsveAAGD 675
Cdd:NF040691   341 LDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGTP-VVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTV---AQDD 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  676 SALSfrVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCmsFVVVLER 755
Cdd:NF040691   417 TAVA--VTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQ--FRLTLPR 492

                   .
gi 2223346070  756 V 756
Cdd:NF040691   493 V 493
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
501-750 2.94e-21

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 99.27  E-value: 2.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  501 QDLQQRQLLMDELQVAKESAdhasrAKSVFLATMSHEIRTPLNAIIGMLELVltRRGETELDHQ-SMHIAYESAVSLLAL 579
Cdd:PRK11360   369 SDLTERKRLQRRVARQERLA-----ALGELVAGVAHEIRNPLTAIRGYVQIW--RQQTSDPPSQeYLSVVLREVDRLNKV 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  580 IGDILDISRiesgKLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDALASAqVWVDAVKVKQIVSNLLSNAIKFT 659
Cdd:PRK11360   442 IDQLLEFSR----PRESQWQPVSLNALVEEVLQLFQTAGVQARVDFETELDNELPP-IWADPELLKQVLLNILINAVQAI 516
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  660 EQGGVdLRCSVEAAGDSALSfrVSVTDTGAGIAAAQLGQVFQPFYVVDGavgdpnAGAGLGLAISQALCLLMGGTLEVKS 739
Cdd:PRK11360   517 SARGK-IRIRTWQYSDGQVA--VSIEDNGCGIDPELLKKIFDPFFTTKA------KGTGLGLALSQRIINAHGGDIEVES 587
                          250
                   ....*....|.
gi 2223346070  740 EEGTGTCMSFV 750
Cdd:PRK11360   588 EPGVGTTFTLY 598
PBP2_BvgS_D1 cd13705
The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
238-453 2.96e-21

The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the first domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a histidine-kinase (HK), a receiver and a histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270423 [Multi-domain]  Cd Length: 221  Bit Score: 93.43  E-value: 2.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  238 GTVRLAVS-EDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVSSLSQANELLDHGAASLsiLPETSPVELPYPH 316
Cdd:cd13705      2 RTLRVGVSaPDYPPFDITSSGGRYEGITADYLGLIADALGVRVEVRRYPDREAALEALRNGEIDL--LGTANGSEAGDGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  317 ---SDPLA-TAPYLFIQRQEAQETLDAQTRATVIIAKGYVEPQQFRAQYPY---LVFKETQtmgEAFKQLRDGGADLVLA 389
Cdd:cd13705     80 lllSQPYLpDQPVLVTRIGDSRQPPPDLAGKRVAVVPGYLPAEEIKQAYPDariVLYPSPL---QALAAVAFGQADYFLG 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2223346070  390 PANVARYYLSYKYESSLKVGGIFDGPGVRIVFAAPHDQAQLISILDKAMLEITPRESLLIVGRW 453
Cdd:cd13705    157 DAISANYLISRNYLNNLRIVRFAPLPSRGFGFAVRPDNTRLLRLLNRALAAIPDEQRDEILRRW 220
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
463-748 3.12e-21

Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 97.63  E-value: 3.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  463 YWEGVASFIWRSFGLLGVMLLVAGMLIVAQRRRIRRKRQDLQQrqllMDELQVAKESAdhasraksvflATMSHEIRTPL 542
Cdd:COG5806    152 ADISELLDFILYFIIIQLLAMLIAVYLIENLIENILLRKELQR----AEKLEVVSELA-----------ASIAHEVRNPL 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  543 NAIIGMLELVLTRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLElapePARMTVLLESVGNVFSGLARQKQ 622
Cdd:COG5806    217 TVVRGFIQLLQEPELSDEKRKQYIRIALEELDRAEAIITDYLTFAKPQPEKLE----KIDVSEELEHVIDVLSPYANMNN 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  623 LRLTLDIDAlaSAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVdLRCSVEAAGDSALsfrVSVTDTGAGIAAAQLGQVFQP 702
Cdd:COG5806    293 VEIQTELEP--GLYIEGDRQKLQQCLINIIKNGIEAMPNGGT-LTIDVSIDKNKVI---ISIKDTGVGMTKEQLERLGEP 366
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2223346070  703 FYVVDGavgdpnAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMS 748
Cdd:COG5806    367 YFSTKE------KGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFT 406
PBP2_BvgS_like_1 cd13708
Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is ...
238-453 3.30e-21

Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270426 [Multi-domain]  Cd Length: 220  Bit Score: 93.34  E-value: 3.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  238 GTVRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVSSLSQANELLDHGAAS-LSILPETsPVELPYPH 316
Cdd:cd13708      2 KEITMCVDPDWMPYEGIDEGGKHVGIAADYLKLIAERLGIPIELVPTKSWSESLEAAKEGKCDiLSLLNQT-PEREEYLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  317 -SDPLATAPYLFIQRQEAQ--ETLDAQTRATVIIAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLVLAPANV 393
Cdd:cd13708     81 fTKPYLSDPNVLVTREDHPfiADLSDLGDKTIGVVKGYAIEEILRQKYPNLNIVEVDSEEEGLKKVSNGELFGFIDSLPV 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2223346070  394 ARYYLSYKYESSLKVGGIFDGP-----GVRivfaapHDQAQLISILDKAMLEITPRESLLIVGRW 453
Cdd:cd13708    161 AAYTIQKEGLFNLKISGKLDEDnelriGVR------KDEPLLLSILNKAIASITPEERQEILNKW 219
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
518-735 4.42e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.59  E-value: 4.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  518 ESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVltRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLELA 597
Cdd:NF012163   231 STLEKNEQMRRDFMADISHELRTPLAVLRAELEAI--QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQ 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  598 PEPARMTVLLESVGNVFSglARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGvDLRCSveaAGDSA 677
Cdd:NF012163   309 KASVDLVPLLEVEGGAFR--ERFASAGLELEVSLPDSSLVFGDRDRLMQLFNNLLENSLRYTDSGG-SLHIS---ASQRP 382
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2223346070  678 LSFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTL 735
Cdd:NF012163   383 KEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTL 440
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
530-750 1.02e-20

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 96.23  E-value: 1.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  530 FLATMSHEIRTPLNAIIGMLELVLTRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLELAPE----PArMTV 605
Cdd:PRK11006   207 FFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKALHTMREQTQRMEGLVKQLLTLSKIEAAPTIDLNEkvdvPM-MLR 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  606 LLESVGNVFSglarQKQLRLTLDIDAlaSAQVWVDAVKVKQIVSNLLSNAIKFTEQGG-VDLRCSVEAAGDsalsfRVSV 684
Cdd:PRK11006   286 VLEREAQTLS----QGKHTITFEVDN--SLKVFGNEDQLRSAISNLVYNAVNHTPEGThITVRWQRVPQGA-----EFSV 354
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2223346070  685 TDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFV 750
Cdd:PRK11006   355 EDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFV 420
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
503-745 4.47e-20

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 94.47  E-value: 4.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  503 LQQRQLLMDELQVAKESAdhasrAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGETELDHQSMHIAYESAVSLLALIGD 582
Cdd:PRK10364   218 LRSRQLLQDEMKRKEKLV-----ALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSE 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  583 ILDISRiesgKLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDI-DALASAQVwvDAVKVKQIVSNLLSNAIKFTEQ 661
Cdd:PRK10364   293 LLELVK----PTHLALQAVDLNDLINHSLQLVSQDANSREIQLRFTAnDTLPEIQA--DPDRLTQVLLNLYLNAIQAIGQ 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  662 GGVdLRCSVEAAGDSAlsfRVSVTDTGAGIAAAQLGQVFQPFYVVDgavgdpNAGAGLGLAISQALCLLMGGTLEVKSEE 741
Cdd:PRK10364   367 HGV-ISVTASESGAGV---KISVTDSGKGIAADQLEAIFTPYFTTK------AEGTGLGLAVVHNIVEQHGGTIQVASQE 436

                   ....
gi 2223346070  742 GTGT 745
Cdd:PRK10364   437 GKGA 440
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
776-889 6.71e-20

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 88.04  E-value: 6.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  776 PLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQqqgGKPCL 855
Cdd:COG3706      1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPR---TADIP 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2223346070  856 IIGLTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:COG3706     78 IIFLTALDDEEDRARALEAGADDYLTKPFDPEEL 111
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
533-744 1.06e-19

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 93.37  E-value: 1.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  533 TMSHEIRTPLNAIIGMLELVLTRRGETELDHQSMHIAYESAvSLLALIGDILDISRIESGKLELAPEPARMTVLLESVGN 612
Cdd:PRK11100   262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSA-RLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVE 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  613 VFSGLARQKQLRLTLDIDALAsaqVWVDAVKVKQIVSNLLSNAIKFTEQGGVdLRCSVEAAGDSAlsfRVSVTDTGAGIA 692
Cdd:PRK11100   341 AREAQAAAKGITLRLRPDDAR---VLGDPFLLRQALGNLLDNAIDFSPEGGT-ITLSAEVDGEQV---ALSVEDQGPGIP 413
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2223346070  693 AAQLGQVFQPFYvvdgAVGDPNAG---AGLGLAISQALCLLMGGTLEVKSEEGTG 744
Cdd:PRK11100   414 DYALPRIFERFY----SLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGG 464
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
779-889 3.35e-19

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 83.74  E-value: 3.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQqggkpCLIIG 858
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT-----TPVII 75
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2223346070  859 LTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:pfam00072   76 LTAHGDEDDAVEALEAGADDFLSKPFDPDEL 106
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
776-889 7.03e-19

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 86.16  E-value: 7.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  776 PLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQqggkpCL 855
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSD-----IP 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2223346070  856 IIGLTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:COG0745     76 IIMLTARDDEEDRVRGLEAGADDYLTKPFDPEEL 109
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
779-889 1.49e-18

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 82.12  E-value: 1.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQqqgGKPCLIIG 858
Cdd:cd17580      1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPW---LANTPAIA 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2223346070  859 LTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:cd17580     78 LTGYGQPEDRERALEAGFDAHLVKPVDPDEL 108
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
775-893 1.61e-18

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 85.60  E-value: 1.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  775 EPLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQqqgGKPC 854
Cdd:COG3437      5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPS---TRDI 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2223346070  855 LIIGLTADAQREALQLCRDAGMDHALAKPTNLATLNRFI 893
Cdd:COG3437     82 PVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARV 120
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
240-453 2.83e-18

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 84.65  E-value: 2.83e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  240 VRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVSSlSQANELLDHG-----AASLSILPETSPVelpY 314
Cdd:COG0834      1 LRVGVDPDYPPFSFRDEDGKLVGFDVDLARAIAKRLGLKVEFVPVPW-DRLIPALQSGkvdliIAGMTITPEREKQ---V 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  315 PHSDPLATAPYLFIQRQEAQE--TLDAQTRATVIIAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLVLAPAN 392
Cdd:COG0834     77 DFSDPYYTSGQVLLVRKDNSGikSLADLKGKTVGVQAGTTYEEYLKKLGPNAEIVEFDSYAEALQALASGRVDAVVTDEP 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2223346070  393 VARYYLSYKYESSLK-VGGIFDGPGVRIVFaaPHDQAQLISILDKAMLEITPRESLL-IVGRW 453
Cdd:COG0834    157 VAAYLLAKNPGDDLKiVGEPLSGEPYGIAV--RKGDPELLEAVNKALAALKADGTLDkILEKW 217
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
527-757 4.18e-18

Cu(+)/Ag(+) sensor histidine kinase;


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 88.68  E-value: 4.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  527 KSVFLATMSHEIRTPLNAIIGMLELVLTR-RGETELDhQSMHIAYESAVSLLALIGDILDISRIESGKLELAPEPARMTV 605
Cdd:PRK09835   262 QSNFSADIAHEIRTPITNLITQTEIALSQsRSQKELE-DVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLAD 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  606 LLESVGNVFSGLARQKQLRLTLDIDAlasAQVWVDAVKVKQIVSNLLSNAIKFTEQG-GVDLRCSveaagDSALSFRVSV 684
Cdd:PRK09835   341 EVGKVFDFFEAWAEERGVELRFVGDP---CQVAGDPLMLRRAISNLLSNALRYTPAGeAITVRCQ-----EVDHQVQLVV 412
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2223346070  685 TDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSE-EGTgtcmSFVVVLERVM 757
Cdd:PRK09835   413 ENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDaRGT----RFVISLPRLE 482
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
640-744 1.49e-17

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 79.07  E-value: 1.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  640 DAVKVKQIVSNLLSNAIKFTEQGGVdLRCSVEAAGDSalSFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGL 719
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTPDGGR-IRCILEKFRLN--RFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGL 77
                           90       100
                   ....*....|....*....|....*
gi 2223346070  720 GLAISQALCLLMGGTLEVKSEEGTG 744
Cdd:cd16925     78 GLSIVKEFVELHGGTVTVSDAPGGG 102
PRK10490 PRK10490
sensor protein KdpD; Provisional
531-756 5.29e-17

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 86.24  E-value: 5.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  531 LATMSHEIRTPLNAIIGMLElVLTRRGETEldhQSMHIAYESAV-----SLLALIGDILDISRIESGKLELAPEparMTV 605
Cdd:PRK10490   668 LAALSHDLRTPLTVLFGQAE-ILTLDLASE---GSPHARQASEIrqqvlNTTRLVNNLLDMARIQSGGFNLRKE---WLT 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  606 LLESVGNVFSGLA-----RQKQLRLTLDIdalasAQVWVDAVKVKQIVSNLLSNAIKFT-EQGGVDLRCSVEAAgdsalS 679
Cdd:PRK10490   741 LEEVVGSALQMLEpglsgHPINLSLPEPL-----TLIHVDGPLFERVLINLLENAVKYAgAQAEIGIDAHVEGE-----R 810
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2223346070  680 FRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPnaGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFVVVLERV 756
Cdd:PRK10490   811 LQLDVWDNGPGIPPGQEQLIFDKFARGNKESAIP--GVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLETP 885
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
780-883 6.22e-17

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 76.88  E-value: 6.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  780 LVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQqggkpCLIIGL 859
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPD-----IPVIVL 75
                           90       100
                   ....*....|....*....|....
gi 2223346070  860 TADAQREALQLCRDAGMDHALAKP 883
Cdd:cd00156     76 TAKADEEDAVRALELGADDYLVKP 99
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
644-753 1.42e-16

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 76.31  E-value: 1.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  644 VKQIVSNLLSNAIKFTEQGGvdlRCSVEAAGDSAlSFRVSVTDTGAGIAAAQLGQVFQPFYVVDgAVGDpnaGAGLGLAI 723
Cdd:cd16943      4 LNQVLLNLLVNAAQAMEGRG---RITIRTWAHVD-QVLIEVEDTGSGIDPEILGRIFDPFFTTK-PVGE---GTGLGLSL 75
                           90       100       110
                   ....*....|....*....|....*....|
gi 2223346070  724 SQALCLLMGGTLEVKSEEGTGTcmSFVVVL 753
Cdd:cd16943     76 SYRIIQKHGGTIRVASVPGGGT--RFTIIL 103
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
526-592 1.66e-16

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 74.56  E-value: 1.66e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2223346070  526 AKSVFLATMSHEIRTPLNAIIGMLELvLTRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESG 592
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLEL-LRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
530-735 3.72e-16

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 82.37  E-value: 3.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  530 FLATMSHEIRTPLNAIIGMLELVltRRGETELDHQSMHiAYESAVSLLA-LIGDILDISRIESGKLELAPEPARMTVLLE 608
Cdd:PRK10549   243 FMADISHELRTPLAVLRGELEAI--QDGVRKFTPESVA-SLQAEVGTLTkLVDDLHQLSLSDEGALAYRKTPVDLVPLLE 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  609 SVGNVFSGLARQKQLRLTLDIDAlaSAQVWVDAVKVKQIVSNLLSNAIKFTEQGGvDLRCSVEAAGDSalsFRVSVTDTG 688
Cdd:PRK10549   320 VAGGAFRERFASRGLTLQLSLPD--SATVFGDPDRLMQLFNNLLENSLRYTDSGG-SLHISAEQRDKT---LRLTFADSA 393
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2223346070  689 AGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTL 735
Cdd:PRK10549   394 PGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRI 440
PBP2_BvgS_D2 cd13707
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
5-196 9.25e-16

The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270425 [Multi-domain]  Cd Length: 221  Bit Score: 77.26  E-value: 9.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070    5 LPPLRIFVEGPRLEGLLADYVVALQRELG---VPIRLRSFltrDAMYAALRGGDLDMVSNINPLMAASHGLVLSPPYVLT 81
Cdd:cd13707     12 LAPLSFFDSNGQFRGISADLLELISLRTGlrfEVVRASSP---AEMIEALRSGEADMIAALTPSPEREDFLLFTRPYLTS 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   82 ELALFSEGGDLHEYSIDD--GQtRIAVANG-MMLELFRSAGGRGRFQHYPSALLAMASVLTGENEVFLGDALSTRYLSSQ 158
Cdd:cd13707     89 PFVLVTRKDAAAPSSLEDlaGK-RVAIPAGsALEDLLRRRYPQIELVEVDNTAEALALVASGKADATVASLISARYLINH 167
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2223346070  159 LFSNQLVVNQSVKLPEVKVGFGLKPGNAILEGILKRAL 196
Cdd:cd13707    168 YFRDRLKIAGILGEPPAPIAFAVRRDQPELLSILDKAL 205
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
644-746 1.36e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 73.25  E-value: 1.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  644 VKQIVSNLLSNAIKFteqGGVDLRCSVEAAGDSAlsfRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGdpNAGAGLGLAI 723
Cdd:cd16950      1 LKRVLSNLVDNALRY---GGGWVEVSSDGEGNRT---RIQVLDNGPGIAPEEVDELFQPFYRGDNARG--TSGTGLGLAI 72
                           90       100
                   ....*....|....*....|...
gi 2223346070  724 SQALCLLMGGTLEVKSEEGTGTC 746
Cdd:cd16950     73 VQRISDAHGGSLTLANRAGGGLC 95
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
504-754 1.76e-15

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 81.52  E-value: 1.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  504 QQRQLLMDE-LQVAKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGETELDHQSMHIAYESAvSLLALIGD 582
Cdd:PRK10618   426 QDREVLVNKkLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSD-VLVRLVDN 504
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  583 ILDISRIESGKLELAPEPARMTVLLESVgnVFSGLARQKQLRLTLDID-ALASAQVWV-DAVKVKQIVSNLLSNAIKFTE 660
Cdd:PRK10618   505 IQLLNMLETQDWKPEQELFSLQDLIDEV--LPEVLPAIKRKGLQLLIHnHLKAEQLRIgDRDALRKILLLLLNYAITTTA 582
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  661 QGGVDLRCSVEAAGDSALSFRVSvtDTGAGIAAAQLGQVFQPFyvVDGAVGDP-NAGAGLGLAISQALCLLMGGTLEVKS 739
Cdd:PRK10618   583 YGKITLEVDQDESSPDRLTIRIL--DTGAGVSIKELDNLHFPF--LNQTQGDRyGKASGLTFFLCNQLCRKLGGHLTIKS 658
                          250
                   ....*....|....*
gi 2223346070  740 EEGTGTCMSFVVVLE 754
Cdd:PRK10618   659 REGLGTRYSIHLKML 673
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
778-883 2.39e-15

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 72.50  E-value: 2.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  778 SVLVVEDHLPS----QYLLVQQVGYlgHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLeqqqgGKP 853
Cdd:COG4753      1 KVLIVDDEPLIreglKRILEWEAGF--EVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIREL-----DPD 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 2223346070  854 CLIIGLTADAQREALQLCRDAGMDHALAKP 883
Cdd:COG4753     74 TKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
640-735 8.86e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 71.34  E-value: 8.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  640 DAVKVKQIVSNLLSNAIKFTEQGG-VDLRCSVEAAGdsalsFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAG 718
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGGkLRIRAAQTPQE-----VRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSG 75
                           90
                   ....*....|....*..
gi 2223346070  719 LGLAISQALCLLMGGTL 735
Cdd:cd16946     76 LGLAICHNIALAHGGTI 92
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
524-588 1.38e-14

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 69.16  E-value: 1.38e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2223346070  524 SRAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGETELDHQSMHIAYESAVSLLALIGDILDISR 588
Cdd:cd00082      1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
526-592 1.63e-14

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 69.13  E-value: 1.63e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2223346070   526 AKSVFLATMSHEIRTPLNAIIGMLELvLTRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESG 592
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLEL-LLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
240-442 2.58e-14

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 73.09  E-value: 2.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  240 VRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVSSlSQANELL-----DHGAASLSILPE-------T 307
Cdd:pfam00497    1 LRVGTDGDYPPFEYVDENGKLVGFDVDLAKAIAKRLGVKVEFVPVSW-DGLIPALqsgkvDLIIAGMTITPErakqvdfS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  308 SPVelpyphsdpLATAPYLFIQRQEAQETLDAQ---TRATVIIAKGYV-EPQQFRAQYPYLVFKETQTMGEAFKQLRDGG 383
Cdd:pfam00497   80 DPY---------YYSGQVILVRKKDSSKSIKSLadlKGKTVGVQKGSTaEELLKNLKLPGAEIVEYDDDAEALQALANGR 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2223346070  384 ADLVLAPANVARYYLSyKYESSLKVGGIFDGPGVRIVFAAPHDQAQLISILDKAMLEIT 442
Cdd:pfam00497  151 VDAVVADSPVAAYLIK-KNPGLNLVVVGEPLSPEPYGIAVRKGDPELLAAVNKALAELK 208
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
632-745 4.05e-14

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 69.36  E-value: 4.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  632 LASAQVWVDAVKVKQIVSNLLSNAIKFTEQGG-VDLRCSveaAGDSALsfrVSVTDTGAGIAAAQLGQVFQPFYVVDGAV 710
Cdd:cd16940      2 AADIQVQGDALLLFLLLRNLVDNAVRYSPQGSrVEIKLS---ADDGAV---IRVEDNGPGIDEEELEALFERFYRSDGQN 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2223346070  711 GDpnaGAGLGLAISQALCLLMGGTLEVKSEEGTGT 745
Cdd:cd16940     76 YG---GSGLGLSIVKRIVELHGGQIFLGNAQGGGL 107
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
644-749 9.47e-14

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 68.19  E-value: 9.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  644 VKQIVSNLLSNAIKFTEQGGV---DLRCSVEAAGDSALSfrVSVTDTGAGIAAAQLGQVFQPFYVVDgavgdpNAGAGLG 720
Cdd:cd16920      1 IQQVLINLVRNGIEAMSEGGCerrELTIRTSPADDRAVT--ISVKDTGPGIAEEVAGQLFDPFYTTK------SEGLGMG 72
                           90       100
                   ....*....|....*....|....*....
gi 2223346070  721 LAISQALCLLMGGTLEVKSEEGTGTCMSF 749
Cdd:cd16920     73 LSICRSIIEAHGGRLSVESPAGGGATFQF 101
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
501-753 9.84e-14

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 74.11  E-value: 9.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  501 QDLQQRQLLMDELQVAKESADhASRAksvflatMSHEIRTPLNAIIGMLELvltrrgeteldhqsmhIAYESAvslLALI 580
Cdd:COG3290    171 RDRTELERLEEELEGVKELAE-ALRA-------QRHDFRNHLHTISGLLQL----------------GEYDEA---LEYI 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  581 GDILDISRIESGKLELAPEPARMTVLLESvgnvFSGLARQKQLRLTLDIDALASAQvWVDAVKVKQIVSNLLSNAIKFTE 660
Cdd:COG3290    224 DEISEELQELIDSLLSRIGNPVLAALLLG----KAARARERGIDLTIDIDSDLPDL-PLSDTDLVTILGNLLDNAIEAVE 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  661 QGGVDLR---CSVEAAGDSalsFRVSVTDTGAGIAAAQLGQVFQPfyvvdGAVGDPNAGAGLGLAISQALCLLMGGTLEV 737
Cdd:COG3290    299 KLPEEERrveLSIRDDGDE---LVIEVEDSGPGIPEELLEKIFER-----GFSTKLGEGRGLGLALVKQIVEKYGGTIEV 370
                          250
                   ....*....|....*.
gi 2223346070  738 KSEEGTGTCmsFVVVL 753
Cdd:COG3290    371 ESEEGEGTV--FTVRL 384
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
6-199 1.78e-13

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 70.78  E-value: 1.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070    6 PPLRIFVEGPRLEGLLADYVVALQRELGVPIRLRsFLTRDAMYAALRGGDLDMVSNINPLMAASHGLVL-SPPYVLTELA 84
Cdd:COG0834     10 PPFSFRDEDGKLVGFDVDLARAIAKRLGLKVEFV-PVPWDRLIPALQSGKVDLIIAGMTITPEREKQVDfSDPYYTSGQV 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   85 LFSEGGDLHEYSIDD--GQtRIAVANG-MMLELFRSAGGRGRFQHYPSALLAMASVLTGENEVFLGDALSTRYLSSQLFS 161
Cdd:COG0834     89 LLVRKDNSGIKSLADlkGK-TVGVQAGtTYEEYLKKLGPNAEIVEFDSYAEALQALASGRVDAVVTDEPVAAYLLAKNPG 167
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2223346070  162 NQLVVNqSVKLPEVKVGFGLKPGNAILEGILKRALGGM 199
Cdd:COG0834    168 DDLKIV-GEPLSGEPYGIAVRKGDPELLEAVNKALAAL 204
PRK10604 PRK10604
sensor protein RstB; Provisional
535-749 2.00e-13

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 73.48  E-value: 2.00e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  535 SHEIRTPLNAIIGMLELVltrRGETELDHQSMHiayESAVSLLALIGDILDISRIESGKLELAPEPARMTVLLESVGNVF 614
Cdd:PRK10604   220 AHELRTPLVRLRYRLEMS---DNLSAAESQALN---RDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAWLSTHLADI 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  615 SGLARQKQLRLtldiDALASAQVW-VDAVKVKQIVSNLLSNAIKFTEQggvDLRCSVEAAGDSALsfrVSVTDTGAGIAA 693
Cdd:PRK10604   294 QAVTPEKTVRL----DTPHQGDYGaLDMRLMERVLDNLLNNALRYAHS---RVRVSLLLDGNQAC---LIVEDDGPGIPP 363
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2223346070  694 AQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSF 749
Cdd:PRK10604   364 EERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSF 419
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
644-749 2.48e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 66.71  E-value: 2.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  644 VKQIVSNLLSNAI-KFTEQGGVDLRCSVEAAGDSALsfrVSVTDTGAGIAAAQLGQVFQPFYVVDgAVGDpnaGAGLGLA 722
Cdd:cd16976      1 IQQVLMNLLQNALdAMGKVENPRIRIAARRLGGRLV---LVVRDNGPGIAEEHLSRVFDPFFTTK-PVGK---GTGLGLS 73
                           90       100
                   ....*....|....*....|....*..
gi 2223346070  723 ISQALCLLMGGTLEVKSEEGTGTCMSF 749
Cdd:cd16976     74 ISYGIVEEHGGRLSVANEEGAGARFTF 100
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
778-883 2.70e-13

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 67.33  E-value: 2.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  778 SVLVVEDHlPSQYLLV----QQVGYlghRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQgGKP 853
Cdd:cd17562      2 KILAVDDS-ASIRQMVsftlRGAGY---EVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYK-FTP 76
                           90       100       110
                   ....*....|....*....|....*....|
gi 2223346070  854 clIIGLTADAQREALQLCRDAGMDHALAKP 883
Cdd:cd17562     77 --ILMLTTESSDEKKQEGKAAGATGWLVKP 104
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
506-889 5.19e-13

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 73.17  E-value: 5.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  506 RQLLMDELQVAKESADHASRAKSV--FLATMSHEIRTPLNAIIGMLELVL-----TRRGETELDH--QSMHIAYEsavsl 576
Cdd:PRK13837   427 RRRLETERDALERRLEHARRLEAVgtLASGIAHNFNNILGAILGYAEMALnklarHSRAARYIDEiiSAGARARL----- 501
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  577 laLIGDILDISRiesgKLELAPEPARmtvLLESVGNVFSGLARQKQLRLTLDID-ALASAQVWVDAVKVKQIVSNLLSNA 655
Cdd:PRK13837   502 --IIDQILAFGR----KGERNTKPFD---LSELVTEIAPLLRVSLPPGVELDFDqDQEPAVVEGNPAELQQVLMNLCSNA 572
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  656 IK-FTEQGGVDLRCSVEA-------------AGDSAlsfRVSVTDTGAGIAAAQLGQVFQPFYVVDgavgdpNAGAGLGL 721
Cdd:PRK13837   573 AQaMDGAGRVDISLSRAKlrapkvlshgvlpPGRYV---LLRVSDTGAGIDEAVLPHIFEPFFTTR------AGGTGLGL 643
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  722 AISQALCLLMGGTLEVKSEEGTGTcmSFVVVLER-----VMADCATLPEGEAPKSHinepLSVLVVEDHLPSQYLLVQQV 796
Cdd:PRK13837   644 ATVHGIVSAHAGYIDVQSTVGRGT--RFDVYLPPsskvpVAPQAFFGPGPLPRGRG----ETVLLVEPDDATLERYEEKL 717
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  797 GYLGHRVlAASNGLEGLATW---SEHAVDIVISDcnMPQMGGLEMARTIRRLeqqqggKPCLIIGLTADAQREALQLCRD 873
Cdd:PRK13837   718 AALGYEP-VGFSTLAAAIAWiskGPERFDLVLVD--DRLLDEEQAAAALHAA------APTLPIILGGNSKTMALSPDLL 788
                          410
                   ....*....|....*.
gi 2223346070  874 AGMDHALAKPTNLATL 889
Cdd:PRK13837   789 ASVAEILAKPISSRTL 804
PRK13557 PRK13557
histidine kinase; Provisional
682-891 8.38e-13

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 72.01  E-value: 8.38e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  682 VSVTDTGAGIAAAQLGQVFQPFYVVDgavgDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTC--MSFVVVLERVMAd 759
Cdd:PRK13557   327 IAVTDTGSGMPPEILARVMDPFFTTK----EEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTvrLYFPASDQAENP- 401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  760 cATLPEGEAPKSHINEplSVLVVEDHLPSQYL---LVQQVGYlghRVLAASNGLEGLATWSEHA-VDIVISDCNMP-QMG 834
Cdd:PRK13557   402 -EQEPKARAIDRGGTE--TILIVDDRPDVAELarmILEDFGY---RTLVASNGREALEILDSHPeVDLLFTDLIMPgGMN 475
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2223346070  835 GLEMARTIRRLEqqqggkPCLIIGLTADAQREALQLCrDAGMDH--ALAKPTNLATLNR 891
Cdd:PRK13557   476 GVMLAREARRRQ------PKIKVLLTTGYAEASIERT-DAGGSEfdILNKPYRRAELAR 527
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
799-897 9.90e-13

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 65.64  E-value: 9.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  799 LGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEmarTIRRLEQQQggKPCLIIGLTADAQREALQLCRDAGMDH 878
Cdd:cd17593     24 WDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYE---VLEALPVEQ--LETKVIVVSGDVQPEAKERVLELGALA 98
                           90
                   ....*....|....*....
gi 2223346070  879 ALAKPTNLATLNRFIPKLG 897
Cdd:cd17593     99 FLKKPFDPEKLAQLLEELG 117
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
775-889 1.24e-12

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 71.15  E-value: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  775 EPLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQqggkpC 854
Cdd:COG2204      1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPD-----L 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2223346070  855 LIIGLTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:COG2204     76 PVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEEL 110
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
775-891 3.27e-12

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 64.99  E-value: 3.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  775 EPLSVLVVEDHLPSQYLLVQQVG-YLGHRVLA-ASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLeqqqgGK 852
Cdd:COG4565      2 KMIRVLIVEDDPMVAELLRRYLErLPGFEVVGvASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRAR-----GP 76
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2223346070  853 PCLIIGLTADAQREALQLCRDAGMDHALAKPTNLATLNR 891
Cdd:COG4565     77 DVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLRE 115
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
644-749 4.67e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 63.22  E-value: 4.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  644 VKQIVSNLLSNAIKFTEQggvDLRCSVEAAGDSAlsfRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAI 723
Cdd:cd16939      1 MARALDNLLRNALRYAHR---TVRIALLVSGGRL---TLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAI 74
                           90       100
                   ....*....|....*....|....*.
gi 2223346070  724 SQALCLLMGGTLEVKSEEGTGTCMSF 749
Cdd:cd16939     75 VHRVALWHGGHVECDDSELGGACFRL 100
PRK09303 PRK09303
histidine kinase;
508-751 5.90e-12

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 68.44  E-value: 5.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  508 LLMDEL-QVAKESADHASR--AKSVFLATMSHEIRTPLNAIIGMLE-LVLTRRGE-TELDHQSMHIAYESAVSLL----A 578
Cdd:PRK09303   129 QLSDELfVLRQENETLLEQlkFKDRVLAMLAHDLRTPLTAASLALEtLELGQIDEdTELKPALIEQLQDQARRQLeeieR 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  579 LIGDILDISRIESGKLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDA-LASaqVWVDAVKVKQIVSNLLSNAIK 657
Cdd:PRK09303   209 LITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSdLPS--VYADQERIRQVLLNLLDNAIK 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  658 FTEQGG-VDL----RCS--VEaagdsalsfrVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPnaGAGLGLAISQALCLL 730
Cdd:PRK09303   287 YTPEGGtITLsmlhRTTqkVQ----------VSICDTGPGIPEEEQERIFEDRVRLPRDEGTE--GYGIGLSVCRRIVRV 354
                          250       260
                   ....*....|....*....|.
gi 2223346070  731 MGGTLEVKSEEGTGTCMSFVV 751
Cdd:PRK09303   355 HYGQIWVDSEPGQGSCFHFTL 375
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
532-745 1.12e-11

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 68.22  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  532 ATMSHEIRTPLNAIIGMLELVltrRGETELDHQSMHIayesavsllaligdILD-ISRIE---SGKLELA-PEPA--RMT 604
Cdd:COG5805    292 AGIAHEIRNPLTSIKGFLQLL---QPGIEDKEEYFDI--------------MLSeLDRIEsiiSEFLALAkPQAVnkEKE 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  605 VLLESVGNVFSGLARQ-----KQLRL-TLDIDalasAQVWVDAVKVKQIVSNLLSNAIKFTEQGGVdLRCSVEAAGDSAl 678
Cdd:COG5805    355 NINELIQDVVTLLETEailhnIQIRLeLLDED----PFIYCDENQIKQVFINLIKNAIEAMPNGGT-ITIHTEEEDNSV- 428
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2223346070  679 sfRVSVTDTGAGIAAAQLGQVFQPFYVVDgavgdpNAGAGLGLAISQALCLLMGGTLEVKSEEGTGT 745
Cdd:COG5805    429 --IIRVIDEGIGIPEERLKKLGEPFFTTK------EKGTGLGLMVSYKIIENHNGTIDIDSKVGKGT 487
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
648-751 1.32e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 62.22  E-value: 1.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  648 VSNLLSNAIKFTEQGG-VDLRCSVEAAGDsalsfRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQA 726
Cdd:cd16952      5 FSNLVSNAVKYTPPSDtITVRWSQEESGA-----RLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKH 79
                           90       100
                   ....*....|....*....|....*
gi 2223346070  727 LCLLMGGTLEVKSEEGTGTCMSFVV 751
Cdd:cd16952     80 VMSRHDARLLIASELGKGSRFTCLF 104
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
1-196 1.69e-11

The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding fold protein; This subfamily includes the periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270422 [Multi-domain]  Cd Length: 220  Bit Score: 64.91  E-value: 1.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070    1 MHDPLPPLRIFVEGPRLEGLLADYVVALQRELGVPIRLRsFLTRDAMYAALRGGDLDMVSNINPLMAASHGLVLSPPYVL 80
Cdd:cd13704      8 GDKNYPPYEFLDENGNPTGFNVDLLRAIAEEMGLKVEIR-LGPWSEVLQALENGEIDVLIGMAYSEERAKLFDFSDPYLE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   81 TELALFSEGGDLHEYSIDD--GQTRIAVANGMMLELFRSAGGRGRFQHYPSALLAMASVLTGENEVFLGDALSTRYLSSQ 158
Cdd:cd13704     87 VSVSIFVRKGSSIINSLEDlkGKKVAVQRGDIMHEYLKERGLGINLVLVDSPEEALRLLASGKVDAAVVDRLVGLYLIKE 166
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2223346070  159 LFSNQLVVNqSVKLPEVKVGFGLKPGNAILEGILKRAL 196
Cdd:cd13704    167 LGLTNVKIV-GPPLLPLKYCFAVRKGNPELLAKLNEGL 203
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
777-896 2.87e-11

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 61.59  E-value: 2.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  777 LSVLVVEDHLPSQYL---LVQQVGYLghRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRlEQQQGGKP 853
Cdd:cd19923      1 MKVLVVDDFSTMRRIiknLLKELGFN--NVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRA-DGALSHLP 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2223346070  854 CLIIglTADAQREALQLCRDAGMDHALAKPTNLATLNRFIPKL 896
Cdd:cd19923     78 VLMV--TAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKI 118
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
776-883 3.36e-11

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 63.44  E-value: 3.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  776 PLSVLVVEDHLPSQYLLVQQVGYLGHRVLA-ASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLeqqqggKPC 854
Cdd:COG3707      3 GLRVLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEE------RPA 76
                           90       100
                   ....*....|....*....|....*....
gi 2223346070  855 LIIGLTADAQREALQLCRDAGMDHALAKP 883
Cdd:COG3707     77 PVILLTAYSDPELIERALEAGVSAYLVKP 105
PRK10610 PRK10610
chemotaxis protein CheY;
774-897 3.75e-11

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 61.53  E-value: 3.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  774 NEPLSVLVVEDHLPSQYL---LVQQVGYlgHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRlEQQQG 850
Cdd:PRK10610     3 DKELKFLVVDDFSTMRRIvrnLLKELGF--NNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRA-DGAMS 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2223346070  851 GKPCLIIglTADAQREALQLCRDAGMDHALAKPTNLAT----LNRFIPKLG 897
Cdd:PRK10610    80 ALPVLMV--TAEAKKENIIAAAQAGASGYVVKPFTAATleekLNKIFEKLG 128
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
650-749 4.07e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 60.80  E-value: 4.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  650 NLLSNAIKFTEQGgVDLRCSVEAAGdsalsFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCL 729
Cdd:cd16949      7 NVLRNALRYSPSK-ILLDISQDGDQ-----WTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAIE 80
                           90       100
                   ....*....|....*....|
gi 2223346070  730 LMGGTLEVKSEEGTGTCMSF 749
Cdd:cd16949     81 QHGGKIKASNRKPGGLRVRI 100
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
779-896 4.07e-11

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 61.20  E-value: 4.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVED----------HLPSQYLLVQQVGylghrvlAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLeqq 848
Cdd:cd17536      1 VLIVDDeplireglkkLIDWEELGFEVVG-------EAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIREL--- 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2223346070  849 qgGKPCLIIGLTADAQ----REALQLcrdaGMDHALAKPTNLATLNRFIPKL 896
Cdd:cd17536     71 --YPDIKIIILSGYDDfeyaQKAIRL----GVVDYLLKPVDEEELEEALEKA 116
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
780-861 5.39e-11

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 60.11  E-value: 5.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  780 LVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQggkPclIIGL 859
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDI---P--IIML 75

                   ..
gi 2223346070  860 TA 861
Cdd:cd17574     76 TA 77
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
644-749 5.53e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 60.42  E-value: 5.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  644 VKQIVSNLLSNAIKFTEQGGVDlrcSVE-AAGDSALSFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAvgDPNAGAGLGLA 722
Cdd:cd16921      1 LGQVLTNLLGNAIKFRRPRRPP---RIEvGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSR--EEYEGTGVGLA 75
                           90       100
                   ....*....|....*....|....*..
gi 2223346070  723 ISQALCLLMGGTLEVKSEEGTGTCMSF 749
Cdd:cd16921     76 IVRKIIERHGGRIWLESEPGEGTTFYF 102
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
779-889 6.16e-11

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 60.63  E-value: 6.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRrleQQQGGKPCLIIG 858
Cdd:cd17548      2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLK---EDPATRDIPVIA 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2223346070  859 LTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:cd17548     79 LTAYAMKGDREKILEAGCDGYISKPIDTREF 109
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
239-441 6.18e-11

Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270248 [Multi-domain]  Cd Length: 217  Bit Score: 63.04  E-value: 6.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  239 TVRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRV--SSLSQA--NELLDHGAASLSILPETS-PVELp 313
Cdd:cd13530      1 TLRVGTDADYPPFEYIDKNGKLVGFDVDLANAIAKRLGVKVEFVDTdfDGLIPAlqSGKIDVAISGMTITPERAkVVDF- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  314 yphSDPLATAPYLFIQRQEAQETLDAQTRATVIIA--KGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLVLAPA 391
Cdd:cd13530     80 ---SDPYYYTGQVLVVKKDSKITKTVADLKGKKVGvqAGTTGEDYAKKNLPNAEVVTYDNYPEALQALKAGRIDAVITDA 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2223346070  392 NVARYYLSyKYESSLKVGGIFDGPGvRIVFAAPHDQAQLISILDKAMLEI 441
Cdd:cd13530    157 PVAKYYVK-KNGPDLKVVGEPLTPE-PYGIAVRKGNPELLDAINKALAEL 204
envZ PRK09467
osmolarity sensor protein; Provisional
531-742 7.66e-11

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 65.32  E-value: 7.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  531 LATMSHEIRTPLnaiigmlelvlTR-RGETELDHQSMHIAYESAVSllaligDILD--------ISRIESGKlELAPEPA 601
Cdd:PRK09467   233 MAGVSHDLRTPL-----------TRiRLATEMMSEEDGYLAESINK------DIEEcnaiieqfIDYLRTGQ-EMPMEMA 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  602 RMTVLLESVGNVFSGlaRQKQLRLTLdidALASAQVWVDAVKVKQIVSNLLSNAIKFTEqGGVDLRCSVEaaGDSAlsfR 681
Cdd:PRK09467   295 DLNALLGEVIAAESG--YEREIETAL---QPGPIEVPMNPIAIKRALANLVVNAARYGN-GWIKVSSGTE--GKRA---W 363
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2223346070  682 VSVTDTGAGIAAAQLGQVFQPFYVVDGAVGdpNAGAGLGLAISQALCLLMGGTLEV-KSEEG 742
Cdd:PRK09467   364 FQVEDDGPGIPPEQLKHLFQPFTRGDSARG--SSGTGLGLAIVKRIVDQHNGKVELgNSEEG 423
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
779-862 1.35e-10

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 59.84  E-value: 1.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEH-AVDIVISDCNMPQMGGLEMARTIRrleQQQGGKPCLII 857
Cdd:cd17544      3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHpDIKLVITDYNMPEMDGFELVREIR---KKYSRDQLAII 79

                   ....*
gi 2223346070  858 GLTAD 862
Cdd:cd17544     80 GISAS 84
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
779-883 1.50e-10

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 59.05  E-value: 1.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMArtiRRLEQQQGGKPCLIIG 858
Cdd:cd17538      2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVC---RRLKEDPETRHIPVIM 78
                           90       100
                   ....*....|....*....|....*
gi 2223346070  859 LTADAQREALQLCRDAGMDHALAKP 883
Cdd:cd17538     79 ITALDDREDRIRGLEAGADDFLSKP 103
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
776-869 2.20e-10

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 61.76  E-value: 2.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  776 PLSVLVVEDHLPSQYLLVQQVG-YLGHRVLA-ASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEqqqggKP 853
Cdd:COG3279      1 MMKILIVDDEPLARERLERLLEkYPDLEVVGeASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELD-----PP 75
                           90
                   ....*....|....*.
gi 2223346070  854 CLIIGLTADAQReALQ 869
Cdd:COG3279     76 PPIIFTTAYDEY-ALE 90
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
779-893 2.73e-10

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 63.71  E-value: 2.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQGgkpclIIG 858
Cdd:PRK11361     7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTP-----VIL 81
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2223346070  859 LTADAQRE-ALQLCRDAGMDHALaKPTNLATLNRFI 893
Cdd:PRK11361    82 MTAYAEVEtAVEALRCGAFDYVI-KPFDLDELNLIV 116
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
239-441 2.94e-10

The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding fold protein; This subfamily includes the periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270422 [Multi-domain]  Cd Length: 220  Bit Score: 61.06  E-value: 2.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  239 TVRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIdRVSSLSQANELLDHGAASLSILPETSPV-ELPYPHS 317
Cdd:cd13704      3 TVIVGGDKNYPPYEFLDENGNPTGFNVDLLRAIAEEMGLKVEI-RLGPWSEVLQALENGEIDVLIGMAYSEErAKLFDFS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  318 DPLATAPYLFIQRQEAQ--ETLDAQTRATVIIAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLVLAPANVAR 395
Cdd:cd13704     82 DPYLEVSVSIFVRKGSSiiNSLEDLKGKKVAVQRGDIMHEYLKERGLGINLVLVDSPEEALRLLASGKVDAAVVDRLVGL 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2223346070  396 YYLSYKYESSLKVGGIFDgPGVRIVFAAPHDQAQLISILDKAMLEI 441
Cdd:cd13704    162 YLIKELGLTNVKIVGPPL-LPLKYCFAVRKGNPELLAKLNEGLAIL 206
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
779-883 5.74e-10

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 57.84  E-value: 5.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLL---VQQVGYlgHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQgGKPcl 855
Cdd:cd17551      3 ILIVDDNPTNLLLLealLRSAGY--LEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLE-DVP-- 77
                           90       100
                   ....*....|....*....|....*...
gi 2223346070  856 IIGLTADAQREALQLCRDAGMDHALAKP 883
Cdd:cd17551     78 IVMITADTDREVRLRALEAGATDFLTKP 105
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
779-883 1.16e-09

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 56.91  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMartIRRLEQQQGGKPCLIig 858
Cdd:cd19934      1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSV---LRRWRSEGRATPVLI-- 75
                           90       100
                   ....*....|....*....|....*.
gi 2223346070  859 LTA-DAQREALQLCrDAGMDHALAKP 883
Cdd:cd19934     76 LTArDSWQDKVEGL-DAGADDYLTKP 100
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
635-739 1.19e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 57.14  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  635 AQVWVDAVKvkQIVSNLLSNAIKFTEQG---GVDLRcsveaagDSALSFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVG 711
Cdd:cd16947     14 ANANTEALQ--RILKNLISNAIKYGSDGkflGMTLR-------EDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRN 84
                           90       100
                   ....*....|....*....|....*...
gi 2223346070  712 DPNAGAGLGLAISQALCLLMGGTLEVKS 739
Cdd:cd16947     85 SAKQGNGLGLTITKRLAESMGGSIYVNS 112
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
779-843 1.37e-09

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 56.57  E-value: 1.37e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHlPSQ-----YLLVQQvgylGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIR 843
Cdd:cd17598      1 ILIVEDS-PTQaeqlkHILEEQ----GYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIK 65
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
796-870 1.54e-09

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 56.44  E-value: 1.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  796 VGYL---GHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQggkPCLII---GLTADAQrEALQ 869
Cdd:cd17555     17 AAYLedsGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDT---PVIVVsgaGVMSDAV-EALR 92

                   .
gi 2223346070  870 L 870
Cdd:cd17555     93 L 93
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
779-889 1.61e-09

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 56.37  E-value: 1.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHlPS-----QYLLVQQvgyLGHRVLA-ASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQqggk 852
Cdd:cd17535      1 VLIVDDH-PLvreglRRLLESE---PDIEVVGeAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPD---- 72
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2223346070  853 pCLIIGLTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:cd17535     73 -LKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEEL 108
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
777-831 1.83e-09

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 54.11  E-value: 1.83e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2223346070   777 LSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMP 831
Cdd:smart00448    1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
647-750 1.96e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 56.14  E-value: 1.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  647 IVSNLLSNAIKFTEQGGvDLRCSVEAAGDSALsfrVSVTDTGAGIAAAQLGQVFQPFYVvdGAVG-DPNAGAGLGLAISQ 725
Cdd:cd16948      9 IIGQIVSNALKYSKQGG-KIEIYSETNEQGVV---LSIKDFGIGIPEEDLPRVFDKGFT--GENGrNFQESTGMGLYLVK 82
                           90       100
                   ....*....|....*....|....*
gi 2223346070  726 ALCLLMGGTLEVKSEEGTGTCMSFV 750
Cdd:cd16948     83 KLCDKLGHKIDVESEVGEGTTFTIT 107
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
777-889 3.88e-09

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 55.48  E-value: 3.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  777 LSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWS--EHAVDIVISDCNMPQMGGLEMARTIRRLEQQQggKPC 854
Cdd:cd19933      1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLAsaEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRR--ERP 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2223346070  855 LIIGLTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:cd19933     79 LIVALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
778-843 5.92e-09

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 54.92  E-value: 5.92e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2223346070  778 SVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIR 843
Cdd:cd17554      2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIR 67
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
640-744 5.97e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 54.39  E-value: 5.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  640 DAVKVKQIVSNLLSNAIKFTEQGGVdLRCSVEAAGDSAlsfRVSVTDTGAGIAAAQLGQVFQPFYvvdgAVGDPNAG--- 716
Cdd:cd16945      1 DPFLLRQAINNLLDNAIDFSPEGGL-IALQLEADTEGI---ELLVFDEGSGIPDYALNRVFERFY----SLPRPHSGqks 72
                           90       100
                   ....*....|....*....|....*...
gi 2223346070  717 AGLGLAISQALCLLMGGTLEVKSEEGTG 744
Cdd:cd16945     73 TGLGLAFVQEVAQLHGGRITLRNRPDGV 100
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
521-755 1.32e-08

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 58.06  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  521 DHASRAKSVFLATMSHEIRTPLNAIigmlelvltrRGETELDHQSMHIAYESAV----SLLALIGDILDISRIE----SG 592
Cdd:PRK10755   131 TSTLDQERLFTADVAHELRTPLAGI----------RLHLELLEKQHHIDVAPLIarldQMMHTVEQLLQLARAGqsfsSG 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  593 KLElapeparmTV-LLESV----GNVFSGLARQKQLRLTLDIDAlASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGvDLR 667
Cdd:PRK10755   201 HYQ--------TVkLLEDVilpsQDELSEMLEQRQQTLLLPESA-ADITVQGDATLLRLLLRNLVENAHRYSPEGS-TIT 270
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  668 CSVEAAGDSAlsfRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGdpnaGAGLGLAISQALCLLMGGTLEVKS-EEGTGTC 746
Cdd:PRK10755   271 IKLSQEDGGA---VLAVEDEGPGIDESKCGELSKAFVRMDSRYG----GIGLGLSIVSRITQLHHGQFFLQNrQERSGTR 343

                   ....*....
gi 2223346070  747 MSfvVVLER 755
Cdd:PRK10755   344 AW--VWLPK 350
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
501-754 2.62e-08

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 57.77  E-value: 2.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  501 QDLQQRQLLMDELQVAKESADHASRAKSV--FLATMSHEIRTPLNAIIGML---ELVLTRRGETELDHQSMHIAyesavS 575
Cdd:COG4192    405 TEIEERKRIEKNLRQTQDELIQAAKMAVVgqTMTSLAHELNQPLNAMSMYLfsaKKALEQENYAQLPTSLDKIE-----G 479
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  576 LLALIGDILDISRIESGKLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDAlasaQVWVDAVKVKQIVSNLLSNA 655
Cdd:COG4192    480 LIERMDKIIKSLRQFSRKSDTPLQPVDLRQVIEQAWELVESRAKPQQITLHIPDDL----MVQGDQVLLEQVLVNLLVNA 555
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  656 IkfteQGGVDLRCSVEAAGDSALSFRVSVTDTGAGIAAAQlgQVFQPFYVvdgavgDPNAGAGLGLAISQALCLLMGGTL 735
Cdd:COG4192    556 L----DAVATQPQISVDLLSNAENLRVAISDNGNGWPLVD--KLFTPFTT------TKEVGLGLGLSICRSIMQQFGGDL 623
                          250
                   ....*....|....*....
gi 2223346070  736 EVKSEEGTGTCmsfvVVLE 754
Cdd:COG4192    624 YLASTLERGAM----VILE 638
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
531-723 3.12e-08

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 57.25  E-value: 3.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  531 LATMSHEIRTPLNAIIGMLELVLTRRGE-TELDHqsmhIAYEsAVSLLALIGDILDISRIESgKLELAPEPARMTVLLES 609
Cdd:PRK09470   247 LSDISHELRTPLTRLQLATALLRRRQGEsKELER----IETE-AQRLDSMINDLLVLSRNQQ-KNHLERETFKANSLWSE 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  610 VGNVFSGLARQKQLRLTLDID-----------ALASAqvwvdavkvkqiVSNLLSNAIKFTEQGgVDLRCSVEAAGdsal 678
Cdd:PRK09470   321 VLEDAKFEAEQMGKSLTVSAPpgpwpingnpnALASA------------LENIVRNALRYSHTK-IEVAFSVDKDG---- 383
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2223346070  679 sFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAI 723
Cdd:PRK09470   384 -LTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAI 427
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
640-751 3.26e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 52.54  E-value: 3.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  640 DAVKVKQIVSNLLSNA---IKFTEQGGVDLRCSVEAAGDSALSfrVSVTDTGAGIAAAQLGQVFQPFyvvdgaVGDPNAG 716
Cdd:cd16944      1 DTTQISQVLTNILKNAaeaIEGRPSDVGEVRIRVEADQDGRIV--LIVCDNGKGFPREMRHRATEPY------VTTRPKG 72
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2223346070  717 AGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFVV 751
Cdd:cd16944     73 TGLGLAIVKKIMEEHGGRISLSNREAGGACIRIIL 107
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
425-1002 4.12e-08

HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 57.36  E-value: 4.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  425 HDQAQLISILDKAMLEITPRESLLIVGRWRANSATDDKYWEGVASFIWRSFGLLGVMLLVAGMLIVAQRRRIRRKRQDLQ 504
Cdd:COG2198    273 LLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALL 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  505 QRQLLMDELQVAKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELVLTRRGETELDHQSMHIAYESAVSLLALIGDIL 584
Cdd:COG2198    353 LLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLLLLLLLLLLLLLL 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  585 DISRIESGKLELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDALASAQVWVDAVKVKQIVSNLLSNAIKFTEQGGV 664
Cdd:COG2198    433 LLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVAAALA 512
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  665 DLRCSVEAAGDSALSFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTG 744
Cdd:COG2198    513 ALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGLLLGGLLLLLLLLLLLLLLLLLL 592
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  745 TCMSFVVVLERVMADCATLPEGEAPKSHINEPLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIV 824
Cdd:COG2198    593 LLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAVLLAAAAAAAALAALDLLL 672
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  825 ISDCNMPQMGGLEMARTIRRLEQQQGGKPCLIIGLTADAQREALQLCRDAGMDHALAKPTNLATLNRFIPKLGPDQSWAS 904
Cdd:COG2198    673 DLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLLLLLLLLLLLLLLLLLAAAAAAA 752
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  905 QGLSWTN----------------DIRASMARQVVASNQEESAALRRALEEGDLPGAGRIAHKLKGTAYLLNHQALLEQCV 968
Cdd:COG2198    753 ASPAAPAlpvldlealrrlggdpELLRELLELFLEELPELLAELRQALAAGDLEALARLAHKLKGSAGNLGAPRLAELAA 832
                          570       580       590
                   ....*....|....*....|....*....|....
gi 2223346070  969 EVEELCSGELTEEFGETVQILLDTLEVITGSLQA 1002
Cdd:COG2198    833 ELEQAARAGDLEEAEELLAELEAELERVLAALEA 866
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
777-883 4.32e-08

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 52.42  E-value: 4.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  777 LSVLVVEDHLPSQYLLVQQVGYLGHRVLA-ASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRrleqqqGGKPCL 855
Cdd:cd19932      1 VRVLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIIT------SENIAP 74
                           90       100
                   ....*....|....*....|....*...
gi 2223346070  856 IIGLTADAQREALQLCRDAGMDHALAKP 883
Cdd:cd19932     75 IVLLTAYSQQDLVERAKEAGAMAYLVKP 102
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
779-883 5.37e-08

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 51.40  E-value: 5.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRrleqQQGGKPclIIG 858
Cdd:cd17620      1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR----EWSAVP--VIV 74
                           90       100
                   ....*....|....*....|....*.
gi 2223346070  859 LTA-DAQREALQLCrDAGMDHALAKP 883
Cdd:cd17620     75 LSArDEESDKIAAL-DAGADDYLTKP 99
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
779-883 7.74e-08

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 51.29  E-value: 7.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRrleqqQGGKPCLIIG 858
Cdd:cd19935      1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLR-----AAGKQTPVLM 75
                           90       100       110
                   ....*....|....*....|....*....|
gi 2223346070  859 LTAdaqREALQ-----LcrDAGMDHALAKP 883
Cdd:cd19935     76 LTA---RDSVEdrvkgL--DLGADDYLVKP 100
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
646-753 1.15e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain.


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 51.03  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  646 QIVSNLLSNAIKFTEQGGVdlRCSVEAAGdSALSFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGDPNAGAGLGLAISQ 725
Cdd:cd16953      3 QVLRNLIGNAISFSPPDTG--RITVSAMP-TGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGLSISR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 2223346070  726 ALCLLMGGTL--EVKSEEGTGTCMSFVVVL 753
Cdd:cd16953     80 QIIEAHGGISvaENHNQPGQVIGARFTVQL 109
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
777-896 1.32e-07

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 51.29  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  777 LSVLVVEDHLPSQYLLVQQVGYLGH-RVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRrlEQQQGGKPCL 855
Cdd:cd17530      1 LRVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLA--ESHSNAAVIL 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2223346070  856 IIGLTADAQREALQLCRDAGMD--HALAKPTNLATLNRFIPKL 896
Cdd:cd17530     79 MSGLDGGILESAETLAGANGLNllGTLSKPFSPEELTELLTKY 121
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
682-748 1.36e-07

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 50.84  E-value: 1.36e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2223346070  682 VSVTDTGAGIAAAQLGQVFQPFYVVDGaVGdpnAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMS 748
Cdd:cd16919     50 LEVSDTGSGMPAEVLRRAFEPFFTTKE-VG---KGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVR 112
PBP2_HisK_like_1 cd13706
Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein; This ...
239-453 1.61e-07

Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein; This group includes periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270424 [Multi-domain]  Cd Length: 219  Bit Score: 52.95  E-value: 1.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  239 TVRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIdRVSSLSQANELLDHGAASLSI-LPETSPVELPYPHS 317
Cdd:cd13706      3 PLVVAMDKDYPPFSFLDEDGEPQGILVDLWRLWSEKTGIPVEF-VLLDWNESLEAVRQGEADVHDgLFKSPEREKYLDFS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  318 DPLATAP-YLFIQRQEAQETLDAQTRATVI--IAKGYVEpQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLVLAPANVA 394
Cdd:cd13706     82 QPIATIDtYLYFHKDLSGITNLSDLKGFRVgvVKGDAEE-EFLRAHGPILSLVYYDNYEAMIEAAKAGEIDVFVADEPVA 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2223346070  395 RYYLsYKYESSLKVGGIFDGPGVRIVFAAPHDQAQLISILDKAMLEITPRESLLIVGRW 453
Cdd:cd13706    161 NYYL-YKYGLPDEFRPAFRLYSGQLHPAVAKGNSALLDLINRGFALISPEELARIERKW 218
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
778-889 2.09e-07

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 50.46  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  778 SVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRrlEQQQGGkpclII 857
Cdd:cd17619      2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR--EQSEVG----II 75
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2223346070  858 GLTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:cd17619     76 LVTGRDDEVDRIVGLEIGADDYVTKPFNPREL 107
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
779-889 2.93e-07

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 50.07  E-value: 2.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRrleqqQGGKPCLIIG 858
Cdd:cd17627      1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLR-----AAGNDLPILV 75
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2223346070  859 LTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:cd17627     76 LTARDSVSDRVAGLDAGADDYLVKPFALEEL 106
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
649-740 3.04e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 49.69  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  649 SNLLSNAIKFTEQggvDLRCSVEAAGDSAlSFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAVGdpNAGAGLGLAISQALC 728
Cdd:cd16923      6 SNLLSNAIKYSPE---NTRIYITSFLTDD-VVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRN--TEGAGLGLSIAKAII 79
                           90
                   ....*....|..
gi 2223346070  729 LLMGGTLEVKSE 740
Cdd:cd16923     80 ELHGGSASAEYD 91
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
646-749 3.14e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 49.77  E-value: 3.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  646 QIVSNLLSNAIKFTEQGGVdlrCSVEAAGDSALsFRVSVTDTGAGIAAAQLGQVFQPFYVVDGAvGDPNAGAGLGLAISQ 725
Cdd:cd16975      7 RALINIISNACQYAPEGGT---VSISIYDEEEY-LYFEIWDNGHGFSEQDLKKALELFYRDDTS-RRSGGHYGMGLYIAK 81
                           90       100
                   ....*....|....*....|....
gi 2223346070  726 ALCLLMGGTLEVKSEEGTGTCMSF 749
Cdd:cd16975     82 NLVEKHGGSLIIENSQKGGAEVTV 105
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
647-753 3.81e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 49.21  E-value: 3.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  647 IVSNLLSNAIK-FTEQGGVDLRCSVEAaGDSALSFRVSVTDTGAGIAAAQLGQVFQpfyvvDGAVGDPNAGAGLGLAISQ 725
Cdd:cd16915      4 IVGNLIDNALDaLAATGAPNKQVEVFL-RDEGDDLVIEVRDTGPGIAPELRDKVFE-----RGVSTKGQGERGIGLALVR 77
                           90       100
                   ....*....|....*....|....*...
gi 2223346070  726 ALCLLMGGTLEVKSEEGTGTCmsFVVVL 753
Cdd:cd16915     78 QSVERLGGSITVESEPGGGTT--FSIRI 103
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
779-883 4.08e-07

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 49.47  E-value: 4.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQqggkpCLIIG 858
Cdd:cd17553      3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDEN-----IRVII 77
                           90       100
                   ....*....|....*....|....*
gi 2223346070  859 LTADAQREALQLCRDAGMDHALAKP 883
Cdd:cd17553     78 MTAYGELDMIQESKELGALTHFAKP 102
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
779-861 5.10e-07

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 49.46  E-value: 5.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQ----YLLvQQVGYLghRVLA-ASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEqqqggKP 853
Cdd:cd17532      1 ALIVDDEPLAReelrYLL-EEHPDI--EIVGeAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLA-----KP 72

                   ....*...
gi 2223346070  854 CLIIGLTA 861
Cdd:cd17532     73 PLIVFVTA 80
PRK10337 PRK10337
sensor protein QseC; Provisional
530-748 5.35e-07

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 53.11  E-value: 5.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  530 FLATMSHEIRTPLNAIIGMLELV-LTRRGETELDH--QSMHIAYESAVSLlalIGDILDISRIESGKLELAPEPARMTVL 606
Cdd:PRK10337   240 FTSDAAHELRSPLAALKVQTEVAqLSDDDPQARKKalLQLHAGIDRATRL---VDQLLTLSRLDSLDNLQDVAEIPLEDL 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  607 LESVGNVFSGLARQKQLRLTLDIDAlasaqvwVDAVKVKQ------IVSNLLSNAIKFTEQGG-VDLRCsveaagdSALS 679
Cdd:PRK10337   317 LQSAVMDIYHTAQQAGIDVRLTLNA-------HPVIRTGQplllslLVRNLLDNAIRYSPQGSvVDVTL-------NARN 382
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2223346070  680 FRvsVTDTGAGIAAAQLGQVFQPFYvvdGAVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMS 748
Cdd:PRK10337   383 FT--VRDNGPGVTPEALARIGERFY---RPPGQEATGSGLGLSIVRRIAKLHGMNVSFGNAPEGGFEAK 446
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
799-845 6.11e-07

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 48.94  E-value: 6.11e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2223346070  799 LGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRL 845
Cdd:cd17569     23 EGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRER 69
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
917-994 6.31e-07

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 48.12  E-value: 6.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  917 MARQVVASNQEESAALRRALEEGDLPGAGRIAHKLKGTAYLLNHQALLEQCVEVEELC---SGELTEEFGETVQILLDTL 993
Cdd:pfam01627    2 LLELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLregELPLDPELLEALRDLLEAL 81

                   .
gi 2223346070  994 E 994
Cdd:pfam01627   82 R 82
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
779-883 7.66e-07

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 48.53  E-value: 7.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGL---------ATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQ 849
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALnklenlakeGNDLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2223346070  850 GGKpclIIGLTADAQREALQLCRDAGMDHALAKP 883
Cdd:cd19924     81 NIP---VILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
779-883 1.21e-06

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 48.40  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRleqQQGGKPCLIIG 858
Cdd:cd17618      3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKR---DEMTRDIPIIM 79
                           90       100
                   ....*....|....*....|....*
gi 2223346070  859 LTADAQREALQLCRDAGMDHALAKP 883
Cdd:cd17618     80 LTARGEEEDKVRGLEAGADDYITKP 104
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
1-201 1.28e-06

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 50.37  E-value: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070    1 MHDPLPPLRIFVEGPRLEGLLADYVVALQRELGVPIRLRsFLTRDAMYAALRGGDLDMVSN---INP----LMAashglv 73
Cdd:pfam00497    5 TDGDYPPFEYVDENGKLVGFDVDLAKAIAKRLGVKVEFV-PVSWDGLIPALQSGKVDLIIAgmtITPerakQVD------ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   74 LSPPYVLTELALF--SEGGDLHEYSIDD--GQTrIAVANGMMLE--LFRSAGGRGRFQHYPSALLAMASVLTGENEVFLG 147
Cdd:pfam00497   78 FSDPYYYSGQVILvrKKDSSKSIKSLADlkGKT-VGVQKGSTAEelLKNLKLPGAEIVEYDDDAEALQALANGRVDAVVA 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2223346070  148 DALSTRYLSSQLfSNQLVVNQSVKLPEVKVGFGLKPGNAILEGILKRALGGMTR 201
Cdd:pfam00497  157 DSPVAAYLIKKN-PGLNLVVVGEPLSPEPYGIAVRKGDPELLAAVNKALAELKA 209
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
779-843 1.29e-06

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 47.89  E-value: 1.29e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIR 843
Cdd:cd19920      1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLK 65
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
777-889 1.39e-06

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 48.01  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  777 LSVLVVEDHLPSQYLLVQQVGYL-GHRVLA-ASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRleqqqGGKPC 854
Cdd:cd19925      1 INVLIVEDDPMVAEIHRAYVEQVpGFTVIGtAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA-----AGHDV 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2223346070  855 LIIGLTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:cd19925     76 DVIVVTAANDVETVREALRLGVVDYLIKPFTFERL 110
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
779-890 1.55e-06

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 47.96  E-value: 1.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHlPSQYLLVQQvgYL---GHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIrrleQQQGGKPCL 855
Cdd:cd17572      1 VLLVEDS-PSLAALYQE--YLsdeGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWI----QERSLPTSV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2223346070  856 IIgLTADAQRE-ALQLCRDAGMDHaLAKPTNLATLN 890
Cdd:cd17572     74 IV-ITAHGSVDiAVEAMRLGAYDF-LEKPFDADRLR 107
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
779-883 1.96e-06

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 47.11  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATW-SEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQggKPCLII 857
Cdd:cd18160      2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLqQGKDIDIVVTDIVMPEMDGIELAREARKIDPDV--KILFIS 79
                           90       100
                   ....*....|....*....|....*.
gi 2223346070  858 GLTADAQREALQLCRDAGMdhaLAKP 883
Cdd:cd18160     80 GGAAAAPELLSDAVGDNAT---LKKP 102
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
646-753 2.57e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 47.01  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  646 QIVSNLLSNAIKFT--EQGGVDLRCSVEAAGDSA-----LSFRVSVTDTGAGIAAAQLGQVFQPFyvVDGAVGdpnaGAG 718
Cdd:cd16918      3 QVFLNLVRNAAQALagSGGEIILRTRTQRQVTLGhprhrLALRVSVIDNGPGIPPDLQDTIFYPM--VSGREN----GTG 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2223346070  719 LGLAISQALCLLMGGTLEVKSEEGtgtCMSFVVVL 753
Cdd:cd16918     77 LGLAIAQNIVSQHGGVIECDSQPG---HTVFSVSL 108
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
233-749 2.58e-06

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 51.06  E-value: 2.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  233 WLDRAGTVRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVSSLSQANELLDHGAASLSILPETSPVEL 312
Cdd:COG3920      1 LLLALLLLLLLALAALLLLAALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  313 PYPHSDPLATAPYLFIQRQEAQETLDAQTRATVIIAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLVLAPAN 392
Cdd:COG3920     81 LLALLVLLLLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  393 VARYYLSYKYESSLKVGGIFDGPGVRIVFAAPHDQAQLISILDKAMLEITPRESLLIVGRWRANSATDDKYWEGVASFIW 472
Cdd:COG3920    161 LLLAEELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  473 RSFGLLGVMLLVAGMLIVAQRRRIRRKRQDLQQRQLLMDELQVAKESADHASRAKSVFLATMSHEIRTPLNAIIGMLELv 552
Cdd:COG3920    241 LERRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRELHHRVKNNLQVVSSLLRL- 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  553 lTRRGETELDHQSMHIAYESAVSLLALIGDILdisrIESGKLElapePARMTVLLESVGNVFSGLARQKQLRLTLDIDAL 632
Cdd:COG3920    320 -QARRADDPEAREALEESQNRIQALALVHELL----YQSEDWE----GVDLRDYLRELLEPLRDSYGGRGIRIELDGPDV 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  633 A-SAQVwvdAVKVKQIVSNLLSNAIKF----TEQGGVDLRCSVEAAGdsalsFRVSVTDTGAGIAAAqlgqvfqpfyvvd 707
Cdd:COG3920    391 ElPADA---AVPLGLILNELVTNALKHaflsGEGGRIRVSWRREDGR-----LRLTVSDNGVGLPED------------- 449
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 2223346070  708 gavGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSF 749
Cdd:COG3920    450 ---VDPPARKGLGLRLIRALVRQLGGTLELDRPEGTRVRITF 488
PRK10816 PRK10816
two-component system response regulator PhoP;
779-886 2.80e-06

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 49.35  E-value: 2.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMartIRRLEQQQGGKPCLIig 858
Cdd:PRK10816     3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSL---IRRWRSNDVSLPILV-- 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2223346070  859 LTAdaqREALQ---LCRDAGMDHALAKPTNL 886
Cdd:PRK10816    78 LTA---RESWQdkvEVLSAGADDYVTKPFHI 105
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
779-885 3.90e-06

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 46.91  E-value: 3.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRrleqqqGGKPCLIIG 858
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELR------KTSQVPVLM 74
                           90       100
                   ....*....|....*....|....*..
gi 2223346070  859 LTADAQREALQLCRDAGMDHALAKPTN 885
Cdd:cd17623     75 LTARGDDIDRILGLELGADDYLPKPFN 101
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
779-883 4.13e-06

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 46.19  E-value: 4.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHA-VDIVISDCNMP-QMGGLEMARTIRRLeqqqggKPCLI 856
Cdd:cd18161      1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPdIDLLVTDVIMPgGMNGSQLAEEARRR------RPDLK 74
                           90       100
                   ....*....|....*....|....*...
gi 2223346070  857 IGLTADAQREALQLCR-DAGMDhALAKP 883
Cdd:cd18161     75 VLLTSGYAENAIEGGDlAPGVD-VLSKP 101
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
779-863 5.00e-06

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 46.58  E-value: 5.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMartIRRLEQQQGGKPCL--- 855
Cdd:cd17615      2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEV---LRRLRADGPDVPVLflt 78
                           90
                   ....*....|....*.
gi 2223346070  856 --------IIGLTADA 863
Cdd:cd17615     79 akdsvedrIAGLTAGG 94
PRK10693 PRK10693
two-component system response regulator RssB;
805-892 5.40e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 49.60  E-value: 5.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  805 AASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMartIRRLEQQQGGKPCLIIGLT---ADAQReALQLcrdaGMDHALA 881
Cdd:PRK10693     2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEF---VEHLRNRGDQTPVLVISATenmADIAK-ALRL----GVQDVLL 73
                           90
                   ....*....|.
gi 2223346070  882 KPtnLATLNRF 892
Cdd:PRK10693    74 KP--VKDLNRL 82
PBP2_AA_binding_like_1 cd13625
Substrate-binding domain of putative amino acid-binding protein; the type 2 ...
236-442 7.39e-06

Substrate-binding domain of putative amino acid-binding protein; the type 2 periplasmic-binding protein fold; This putative amino acid-binding protein belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270343 [Multi-domain]  Cd Length: 230  Bit Score: 48.14  E-value: 7.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  236 RAGTVRLAVSEDLAPYAFFNNrGRFNGIASDVLDIIRRKTGLHFKIDRVSSLSQANELL----DHGAASLSILPETSPVe 311
Cdd:cd13625      3 KRGTITVATEADYAPFEFVEN-GKIVGFDRDLLDEMAKKLGVKVEQQDLPWSGILPGLLagkfDMVATSVTITKERAKR- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  312 lpYPHSDPLATAPYLFIQRQ--EAQETLDAQTRATVIIAKGY-VEPQ--QFRAQYP------YLVFKETQTMGEAFKQLR 380
Cdd:cd13625     81 --FAFTLPIAEATAALLKRAgdDSIKTIEDLAGKVVGVQAGSaQLAQlkEFNETLKkkggngFGEIKEYVSYPQAYADLA 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2223346070  381 DGGADLVLAPANVARYYLSYKYESSLKVGGIfdGPGVRIVFAAPHDQAQLISILDKAMLEIT 442
Cdd:cd13625    159 NGRVDAVANSLTNLAYLIKQRPGVFALVGPV--GGPTYFAWVIRKGDAELRKAINDALLALK 218
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
780-861 8.45e-06

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 45.73  E-value: 8.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  780 LVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQgGKPclIIGL 859
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTS-SIP--IIML 77

                   ..
gi 2223346070  860 TA 861
Cdd:cd19937     78 TA 79
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
779-889 8.58e-06

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 45.90  E-value: 8.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQggkpclIIG 858
Cdd:cd17594      2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSDVP------III 75
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2223346070  859 LTADA-QREALQLCRDAGMDHALAKPTNLATL 889
Cdd:cd17594     76 ISGDRrDEIDRVVGLELGADDYLAKPFGLREL 107
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
776-842 1.22e-05

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 45.65  E-value: 1.22e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2223346070  776 PLSVLVVEDHLPS----QYLLVQQVGYlgHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTI 842
Cdd:COG2197      1 MIRVLIVDDHPLVreglRALLEAEPDI--EVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
775-889 1.60e-05

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 46.45  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  775 EPLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQqggkpC 854
Cdd:COG4567      3 EDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPD-----A 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2223346070  855 LIIGLTADAQRE-ALQLCRdAGMDHALAKPTNLATL 889
Cdd:COG4567     78 RIVVLTGYASIAtAVEAIK-LGADDYLAKPADADDL 112
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
640-754 2.61e-05

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 44.18  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  640 DAVKVKQIVSNLLSNAIKFT--EQGGVDLRCS--VEAAGDSA----LSFRvsVTDTGAGIAAAQLGQVFqpfyvvdgavg 711
Cdd:cd16932      3 DQIRLQQVLADFLLNAVRFTpsPGGWVEIKVSptKKQIGDGVhvihLEFR--ITHPGQGLPEELVQEMF----------- 69
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2223346070  712 DPNAGA---GLGLAISQALCLLMGGTLEVKSEEGTGtcmSFVVVLE 754
Cdd:cd16932     70 EENQWTtqeGLGLSISRKLVKLMNGDVRYLREAGRS---YFLITLE 112
PBP2_Cysteine cd13694
Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein ...
231-385 3.16e-05

Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein fold; This subfamily comprises of the periplasmic-binding protein component of ABC transporter specific for cysteine and its closely related proteins. The cysteine-binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270412 [Multi-domain]  Cd Length: 229  Bit Score: 46.58  E-value: 3.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  231 LDWLDRAGTVRLAVSEDLAPYAFFNNRGRFNGIASDVLD-IIRRKTGLHFKI--------DRVSSLSQANelLDHGAASL 301
Cdd:cd13694      1 LEQIKQSGVIRIGVFGDKPPFGYVDENGKFQGFDIDLAKqIAKDLFGSGVKVefvlveaaNRVPYLTSGK--VDLILANF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  302 SILPETSPVeLPYphsdplaTAPYL-----FIQRQEAQETLDAQTRA-TVIIAKGYVEPQQFRAQYPYLVFKETQTMGEA 375
Cdd:cd13694     79 TVTPERAEV-VDF-------ANPYMkvalgVVSPKDSNITSVAQLDGkTLLVNKGTTAEKYFTKNHPEIKLLKYDQNAEA 150
                          170
                   ....*....|
gi 2223346070  376 FKQLRDGGAD 385
Cdd:cd13694    151 FQALKDGRAD 160
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
779-844 3.80e-05

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 44.02  E-value: 3.80e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRR 844
Cdd:cd17550      1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKE 66
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
803-890 3.83e-05

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 44.30  E-value: 3.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  803 VLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLeqqqggKPCLIIGLTADAQR------EALqlcrDAGM 876
Cdd:cd17541     29 VGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE------RPTPVVMVSSLTEEgaeitlEAL----ELGA 98
                           90
                   ....*....|....
gi 2223346070  877 DHALAKPTNLATLN 890
Cdd:cd17541     99 VDFIAKPSGGISLD 112
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
618-745 4.35e-05

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 47.22  E-value: 4.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  618 ARQKQLRLTLDIDAL----ASAQVWVDAVKVkqiVSNLLSNAIK-FTEQGGVDLRCSVEAaGDSALSFRVSvtDTGAGIA 692
Cdd:PRK11086   407 ARELGITLIISEDSQlpdsGDEDQVHELITI---LGNLIENALEaVGGEEGGEISVSLHY-RNGWLHCEVS--DDGPGIA 480
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2223346070  693 AAQLGQVFQPFYVVDGavgdPNAGAGLGLAISQALCLlmGGTLEVKSEEGTGT 745
Cdd:PRK11086   481 PDEIDAIFDKGYSTKG----SNRGVGLYLVKQSVENL--GGSIAVESEPGVGT 527
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
780-889 4.41e-05

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 43.75  E-value: 4.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  780 LVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMartIRRLEQQQGGKPCLIigL 859
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEV---LKSLREEGIETPVLL--L 75
                           90       100       110
                   ....*....|....*....|....*....|
gi 2223346070  860 TADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:cd17625     76 TALDAVEDRVKGLDLGADDYLPKPFSLAEL 105
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
779-845 4.45e-05

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 44.02  E-value: 4.45e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDhlpSQYLL--VQQVGYL-GHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRL 845
Cdd:cd17549      1 VLLVDD---DADVReaLQQTLELaGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIREL 67
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
779-883 5.49e-05

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 43.63  E-value: 5.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRrleqqQGGKPCLIIG 858
Cdd:cd17624      1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWR-----RQGQSLPVLI 75
                           90       100
                   ....*....|....*....|....*...
gi 2223346070  859 LTAdaqREALQ---LCRDAGMDHALAKP 883
Cdd:cd17624     76 LTA---RDGVDdrvAGLDAGADDYLVKP 100
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
800-889 6.08e-05

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 43.31  E-value: 6.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  800 GHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEmarTIRRLEQQQGGKPCLIIGLTADAQREALQLCRDAGMDHA 879
Cdd:cd17552     26 GWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLA---TLKKLQANPETQSIPVILLTAKAQPSDRQRFASLGVAGV 102
                           90
                   ....*....|
gi 2223346070  880 LAKPTNLATL 889
Cdd:cd17552    103 IAKPFDPLTL 112
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
773-895 6.59e-05

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 46.56  E-value: 6.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  773 INEPLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQqqgGK 852
Cdd:PRK10365     2 THDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNP---AI 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2223346070  853 PCLIigLTADAQRE-ALQLCRDAGMDHaLAKPTNLATLNRFIPK 895
Cdd:PRK10365    79 PVLI--MTAYSSVEtAVEALKTGALDY-LIKPLDFDNLQATLEK 119
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
774-843 9.12e-05

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 45.02  E-value: 9.12e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2223346070  774 NEPLSVLVVEDHLPSQYLLVQQVGYL-GHRVLA-ASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIR 843
Cdd:PRK10651     4 QEPATILLIDDHPMLRTGVKQLISMApDITVVGeASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLR 75
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
779-883 1.36e-04

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 42.27  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLL---VQQVGYlgHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQGgkpcl 855
Cdd:cd17542      3 VLIVDDAAFMRMMLkdiLTKAGY--EVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAK----- 75
                           90       100
                   ....*....|....*....|....*...
gi 2223346070  856 IIGLTADAQREALQLCRDAGMDHALAKP 883
Cdd:cd17542     76 VIMCSAMGQEEMVKEAIKAGAKDFIVKP 103
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
798-883 1.82e-04

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 41.59  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  798 YLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMartIRRLEQQQGGKPCLIIGLTADAQREALQLCRDAGMD 877
Cdd:cd19927     20 DQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSL---LGKLRKNADFDTIPVIFLTAKGMTSDRIKGYNAGCD 96

                   ....*.
gi 2223346070  878 HALAKP 883
Cdd:cd19927     97 GYLSKP 102
PBP2_HisJ_LAO_like cd01001
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ...
237-441 1.90e-04

Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and related proteins; the type 2 periplasmic-binding protein fold; This family comprises the periplasmic substrate-binding proteins, including the lysine-, arginine-, ornithine-binding protein (LAO) and the histidine-binding protein (HisJ), which serve as initial receptors for active transport. HisJ and LAO proteins belong to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270222 [Multi-domain]  Cd Length: 228  Bit Score: 43.82  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  237 AGTVRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKIDRVS------SLsQANElLDHGAASLSILPETSPV 310
Cdd:cd01001      1 ADTLRIGTEGDYPPFNFLDADGKLVGFDIDLANALCKRMKVKCEIVTQPwdglipAL-KAGK-YDAIIASMSITDKRRQQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  311 elpYPHSDPLATAPYLFIQRQEA--QETLDAQTRATVI-IAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGGADLV 387
Cdd:cd01001     79 ---IDFTDPYYRTPSRFVARKDSpiTDTTPAKLKGKRVgVQAGTTHEAYLRDRFPEADLVEYDTPEEAYKDLAAGRLDAV 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2223346070  388 LAPANVARYYLS-------YKYESSLKVGGIFDGPGVRIvfAAPHDQAQLISILDKAMLEI 441
Cdd:cd01001    156 FGDKVALSEWLKktksggcCKFVGPAVPDPKYFGDGVGI--AVRKDDDALRAKLDKALAAL 214
PRK11173 PRK11173
two-component response regulator; Provisional
779-843 1.92e-04

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 44.24  E-value: 1.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIR 843
Cdd:PRK11173     6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELR 70
PRK15115 PRK15115
response regulator GlrR; Provisional
773-861 2.35e-04

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 44.83  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  773 INEPLSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRleqQQGGK 852
Cdd:PRK15115     2 SRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQK---VQPGM 78

                   ....*....
gi 2223346070  853 PCLIigLTA 861
Cdd:PRK15115    79 PVII--LTA 85
orf27 CHL00148
Ycf27; Reviewed
779-861 4.79e-04

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 42.78  E-value: 4.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRleqqQGGKPclIIG 858
Cdd:CHL00148     9 ILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK----ESDVP--IIM 82

                   ...
gi 2223346070  859 LTA 861
Cdd:CHL00148    83 LTA 85
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
646-745 4.81e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 39.84  E-value: 4.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  646 QIVSNLLSNAIKFTEQGGVDLRCSVEAAGdsalsFRVSVTDTGAGIAAaqlgqvfqpfyvvdgavGDPNAGAGLGLAISQ 725
Cdd:cd16917      3 RIVQEALTNALKHAGASRVRVTLSYTADE-----LTLTVVDDGVGFDG-----------------PAPPGGGGFGLLGMR 60
                           90       100
                   ....*....|....*....|
gi 2223346070  726 ALCLLMGGTLEVKSEEGTGT 745
Cdd:cd16917     61 ERAELLGGTLTIGSRPGGGT 80
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
779-843 6.10e-04

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 40.26  E-value: 6.10e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2223346070  779 VLVVEDHL----PSQYLLVQQvgylGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIR 843
Cdd:cd17621      1 VLVVEDEEsfsdPLAYLLRKE----GFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR 65
PBP2_BvgS_like_1 cd13708
Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is ...
3-211 8.44e-04

Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270426 [Multi-domain]  Cd Length: 220  Bit Score: 42.11  E-value: 8.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070    3 DP-LPPLRIFVEGPRLEGLLADYVVALQRELGVPIRLRSFLTRDAMYAALRGGDLDMVSNINPLMAASHGLVLSPPYVLT 81
Cdd:cd13708      9 DPdWMPYEGIDEGGKHVGIAADYLKLIAERLGIPIELVPTKSWSESLEAAKEGKCDILSLLNQTPEREEYLNFTKPYLSD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   82 ELALFSEGGdlHEYsIDD----GQTRIAVANG-MMLELFRsaggrgrfQHYP--------SALLAMASVLTGENEVFLGD 148
Cdd:cd13708     89 PNVLVTRED--HPF-IADlsdlGDKTIGVVKGyAIEEILR--------QKYPnlnivevdSEEEGLKKVSNGELFGFIDS 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2223346070  149 ALSTRYLSSQLFSNQLVVnqSVKLPEV-KVGFGLKPGNAILEGILKRALGGMTRCQKIRAQHLW 211
Cdd:cd13708    158 LPVAAYTIQKEGLFNLKI--SGKLDEDnELRIGVRKDEPLLLSILNKAIASITPEERQEILNKW 219
glnL PRK11073
nitrogen regulation protein NR(II);
504-742 8.89e-04

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 42.76  E-value: 8.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  504 QQRQLLMDELQVAKESAdhasrAKsVFLATMSHEIRTPLNAIIG---MLELVLTRRGETELdhqsMHIAYESAVSLLALI 580
Cdd:PRK11073   113 NQRRLSQEQLQHAQQVA-----AR-DLVRGLAHEIKNPLGGLRGaaqLLSKALPDPALTEY----TKVIIEQADRLRNLV 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  581 GDILDISR-----IESgkLELAPEPARMTVLLESVGNVfsglarqkqlRLTLDIDAlASAQVWVDAVKVKQIVSNLLSNA 655
Cdd:PRK11073   183 DRLLGPQRpgthvTES--IHKVAERVVQLVSLELPDNV----------RLIRDYDP-SLPELAHDPDQIEQVLLNIVRNA 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  656 IK-FTEQGG-VDLRC----SVEAAGDS-ALSFRVSVTDTGAGIAAAQLGQVFQPfyVVDGAVGdpnaGAGLGLAISQALC 728
Cdd:PRK11073   250 LQaLGPEGGtITLRTrtafQLTLHGERyRLAARIDIEDNGPGIPPHLQDTLFYP--MVSGREG----GTGLGLSIARNLI 323
                          250
                   ....*....|....
gi 2223346070  729 LLMGGTLEVKSEEG 742
Cdd:PRK11073   324 DQHSGKIEFTSWPG 337
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
17-185 9.75e-04

Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270248 [Multi-domain]  Cd Length: 217  Bit Score: 41.85  E-value: 9.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   17 LEGLLADYVVALQRELGVPIRLRSFlTRDAMYAALRGGDLDMVsninplmAASHG--------LVLSPPYVLTELALFSE 88
Cdd:cd13530     22 LVGFDVDLANAIAKRLGVKVEFVDT-DFDGLIPALQSGKIDVA-------ISGMTitperakvVDFSDPYYYTGQVLVVK 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070   89 GGDLHEYSIDD-GQTRIAVANG-MMLELFRSAGGRGRFQHYPSALLAMASVLTGENEVFLGDALSTRYLSSQLFSNqLVV 166
Cdd:cd13530     94 KDSKITKTVADlKGKKVGVQAGtTGEDYAKKNLPNAEVVTYDNYPEALQALKAGRIDAVITDAPVAKYYVKKNGPD-LKV 172
                          170
                   ....*....|....*....
gi 2223346070  167 NQSVKLPEvKVGFGLKPGN 185
Cdd:cd13530    173 VGEPLTPE-PYGIAVRKGN 190
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
778-897 1.02e-03

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 40.09  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  778 SVLVVEDHlPSQYLLVQQV---GYLGHRVLAASNGLEGLA------TWSEHAV-DIVISDCNMPQMGGLEMARTIRrleQ 847
Cdd:cd17557      1 TILLVEDN-PGDAELIQEAfkeAGVPNELHVVRDGEEALDflrgegEYADAPRpDLILLDLNMPRMDGFEVLREIK---A 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2223346070  848 QQGGKPCLIIGLTADAQREALQLCRDAGMDHALAKPTNLATLNRFIPKLG 897
Cdd:cd17557     77 DPDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLG 126
PBP2_Cys_DEBP_like cd01000
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ...
231-437 1.03e-03

Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 periplasmic-binding protein fold; This family comprises of the periplasmic-binding protein component of ABC transporters specific for cysteine and carboxylic amino acids, as well as their closely related proteins. The cysteine and aspartate-glutamate binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270221 [Multi-domain]  Cd Length: 228  Bit Score: 41.91  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  231 LDWLDRAGTVRLAVSEDLAPYAFFNNRGRFNGIASDVL-DIIRRKTGLHFKI--------DRVSSLsQANElLDHGAASL 301
Cdd:cd01000      1 LDDIKSRGVLIVGVKPDLPPFGARDANGKIQGFDVDVAkALAKDLLGDPVKVkfvpvtsaNRIPAL-QSGK-VDLIIATM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  302 SILPETSPVelpYPHSDP-LATAPYLFIQRQEAQETLDAQTRATVIIAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLR 380
Cdd:cd01000     79 TITPERAKE---VDFSVPyYADGQGLLVRKDSKIKSLEDLKGKTILVLQGSTAEAALRKAAPEAQLLEFDDYAEAFQALE 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2223346070  381 DGGADLVLAPANVARYYLSYKYESSLKVGGIFD----GPGVRivfaapHDQAQLISILDKA 437
Cdd:cd01000    156 SGRVDAMATDNSLLAGWAAENPDDYVILPKPFSqepyGIAVR------KGDTELLKAVNAT 210
PRK10643 PRK10643
two-component system response regulator PmrA;
779-928 1.03e-03

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 41.56  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQggkPCLIig 858
Cdd:PRK10643     3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTL---PVLI-- 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2223346070  859 LTAdaqREALQ-----LcrDAGMDHALAKPTNLATLNRFIPKLGPDQSWASQGLSWTNDIRASMARQVVASNQEE 928
Cdd:PRK10643    78 LTA---RDTLEdrvagL--DVGADDYLVKPFALEELHARIRALIRRHQGQGENELQVGNLTLNLGRQQVWLDGQE 147
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
803-843 1.16e-03

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 39.56  E-value: 1.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2223346070  803 VLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIR 843
Cdd:cd19930     27 VAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELR 67
PRK10766 PRK10766
two-component system response regulator TorR;
778-843 1.94e-03

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 40.79  E-value: 1.94e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2223346070  778 SVLVVEDHLPSQYLLVqqvGYL---GHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIR 843
Cdd:PRK10766     4 HILVVEDEPVTRARLQ---GYFeqeGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR 69
PBP2_Atu4678_like cd13696
The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ...
231-435 2.02e-03

The substrate binding domain of putative amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Agrobacterium tumefaciens and its related proteins. The putative Atu4678-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270414 [Multi-domain]  Cd Length: 227  Bit Score: 40.82  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  231 LDWLDRAGTVRLAVSEDLAPYAFFNNRGRFNGIASDVLDIIRRKTGLHFKI------DRVSSLsQANELlDHGAASLSIL 304
Cdd:cd13696      1 LDDILSSGKLRCGVCLDFPPFGFRDAAGNPVGYDVDYAKDLAKALGVKPEIvetpspNRIPAL-VSGRV-DVVVANTTRT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  305 PETSpveLPYPHSDP-LATAPYLFIQRQEAQETLDAQTRATVIIAKGYVEPQQFRAQYPYLVFKETQTMGEAFKQLRDGG 383
Cdd:cd13696     79 LERA---KTVAFSIPyVVAGMVVLTRKDSGIKSFDDLKGKTVGVVKGSTNEAAVRALLPDAKIQEYDTSADAILALKQGQ 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2223346070  384 ADLVLAPANVARYYLSYKYESSLKVGGIFDGPGVRIVFAAPHDQAQLISILD 435
Cdd:cd13696    156 ADAMVEDNTVANYKASSGQFPSLEIAGEAPYPLDYVAIGVRKGDYDWLRYLN 207
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
778-869 2.19e-03

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 38.93  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  778 SVLVVEDHLPSQYLLVQQVGYLGHRVLA-ASNGLEGLATWSEHAVDIVISDCNMP-QMGGLEMARTIRrleqQQGGKPcl 855
Cdd:cd17534      2 KILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIR----EKFDIP-- 75
                           90
                   ....*....|....
gi 2223346070  856 IIGLTADAQREALQ 869
Cdd:cd17534     76 VIFLTAYSDEETLE 89
PRK11517 PRK11517
DNA-binding response regulator HprR;
777-889 2.20e-03

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 40.65  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  777 LSVLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQggkpclI 856
Cdd:PRK11517     1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQTP------V 74
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2223346070  857 IGLTADAQREALQLCRDAGMDHALAKPTNLATL 889
Cdd:PRK11517    75 ICLTARDSVDDRVRGLDSGANDYLVKPFSFSEL 107
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
779-883 2.71e-03

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 38.56  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRLEQQQggkpclIIG 858
Cdd:cd17614      1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNVP------IIM 74
                           90       100
                   ....*....|....*....|....*
gi 2223346070  859 LTADAQREALQLCRDAGMDHALAKP 883
Cdd:cd17614     75 LTAKDSEVDKVLGLELGADDYVTKP 99
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
606-748 2.80e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain.


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 39.15  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  606 LLESVGNVFSGLARQKQLRLTLDIDAlaSAQVWVDAVKVKQIVSNLLSNAIKFTEqGGVDLrCSVEAAGDsalsFRVSVT 685
Cdd:cd16954      2 LLDSLCSALNKVYQRKGVSISLDISP--ELRFPGERNDLMELLGNLLDNACKWCL-EFVEV-TARQTDGG----LHLIVD 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2223346070  686 DTGAGIAAAQLGQVFQPFYVVDGAVgdpnAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMS 748
Cdd:cd16954     74 DDGPGVPESQRSKIFQRGQRLDEQR----PGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFE 132
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
915-996 3.04e-03

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 37.75  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  915 ASMARQVVASNQEESAALRRALEE----GDLPGAGRIAHKLKGTAYLLNHQALLEQCVEVEELCSG--ELTEEFGETVQI 988
Cdd:cd00088      2 EELLELFLEEAEELLEELERALLEledaEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDAlrDGLEVTPELIDL 81

                   ....*...
gi 2223346070  989 LLDTLEVI 996
Cdd:cd00088     82 LLDALDAL 89
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
530-746 3.34e-03

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 41.27  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  530 FLATMSHEIRTPLNAIIGMLELvLTRRGETELDHQSMHIAYESAVSLLALIGDILDISRIESGKLELAPEPARMTVLLES 609
Cdd:TIGR03785  488 MSSRLSHELRTPVAVVRSSLEN-LELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLSG 566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  610 VGNVFSGLARQKQLRLTLDIDAL---ASAQVWVdavkvkQIVSNLLSNAIKFTEQGGVdLRCSVEAAGDSALsfrVSVTD 686
Cdd:TIGR03785  567 CMQGYQMTYPPQRFELNIPETPLvmrGSPELIA------QMLDKLVDNAREFSPEDGL-IEVGLSQNKSHAL---LTVSN 636
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2223346070  687 TGAGIAAAQLGQVFQPFYVV--DGAVGDPNagAGLGLAISQALCLLMGGTLEVKS-EEGTGTC 746
Cdd:TIGR03785  637 EGPPLPEDMGEQLFDSMVSVrdQGAQDQPH--LGLGLYIVRLIADFHQGRIQAENrQQNDGVV 697
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
640-751 3.70e-03

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 38.59  E-value: 3.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  640 DAVKVKQIVSNLLSNAIKFTEQGG-----VDL------RCSVEAA--------GDSALSFRVSVTDTGAGIAAaqlgQVF 700
Cdd:cd16938      8 DERRVFQVLLHMLGNLLKMRNGGGnitfrVFLeggsedRSDRDWGpwrpsmsdESVEIRFEVEINDSGSPSIE----SAS 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2223346070  701 QPFYVVDGaVGDPNAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFVV 751
Cdd:cd16938     84 MRNSLNRR-YNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
917-971 3.72e-03

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 37.61  E-value: 3.72e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2223346070   917 MARQVVASNQEESAALRRALEEGDLPGAGRIAHKLKGTAYLLNHQALLEQCVEVE 971
Cdd:smart00073    9 ELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLE 63
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
475-751 4.95e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 39.99  E-value: 4.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  475 FGLLGVMLLVAGMLIVAQRRRIRRKRQDLQQRQLLMDELQVAKESADHASRAKsvflatMSHEIR-TPLNAIIGM-LELV 552
Cdd:COG4585      4 LALLGALALLVGALLGLLLALVLLRARRAERAAELERELAARAEEAREEERRR------IARELHdGVGQSLSAIkLQLE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  553 LTRRGETELDHQSMHIAYESAVSLLALIGDILDISRiesgklELAPEPARMTVLLESVGNVFSGLARQKQLRLTLDIDAL 632
Cdd:COG4585     78 AARRLLDADPEAAREELEEIRELAREALAELRRLVR------GLRPPALDDLGLAAALEELAERLLRAAGIRVELDVDGD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  633 A---SAQVWVDAVkvkQIVSNLLSNAIKFTEQGGVDLRCSVEAAGdsalsFRVSVTDTGAGIAAAQLgqvfqpfyvvdga 709
Cdd:COG4585    152 PdrlPPEVELALY---RIVQEALTNALKHAGATRVTVTLEVDDGE-----LTLTVRDDGVGFDPEAA------------- 210
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2223346070  710 vgdpnAGAGLGLAISQALCLLMGGTLEVKSEEGTGTCMSFVV 751
Cdd:COG4585    211 -----PGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATL 247
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
806-889 5.89e-03

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 37.71  E-value: 5.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  806 ASNGLEGLATWSEHAVDIVISDCNMPQMGGLEmarTIRRLEQQqgGKPCLIIGLT-ADAQREALQLCRdAGMDHALAKPT 884
Cdd:cd19931     30 ASSGEEGIELAERLDPDLILLDLNMKGMSGLD---TLKALREE--GVSARIVILTvSDAEDDVVTALR-AGADGYLLKDM 103

                   ....*
gi 2223346070  885 NLATL 889
Cdd:cd19931    104 EPEDL 108
pleD PRK09581
response regulator PleD; Reviewed
803-843 5.91e-03

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 40.27  E-value: 5.91e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2223346070  803 VLAASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIR 843
Cdd:PRK09581    29 VLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLK 69
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
776-882 6.30e-03

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 39.45  E-value: 6.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223346070  776 PLSVLVVEDHlPSQYLLVQQVGYL--GHRVLA-ASNGLEGLATWSEHAVDIVISDCNMPQMGGLEMARTIRRleqqQGGK 852
Cdd:PRK10403     6 PFQVLIVDDH-PLMRRGVRQLLELdpGFEVVAeAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRR----DGVT 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2223346070  853 PCLIIGLTADAQREALQLCrDAGMDHALAK 882
Cdd:PRK10403    81 AQIIILTVSDASSDVFALI-DAGADGYLLK 109
PRK09483 PRK09483
response regulator; Provisional
777-844 6.58e-03

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 39.32  E-value: 6.58e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2223346070  777 LSVLVVEDHLpsqylLVQqVGYL-------GHRVLAASNGLEGLATWS-EHAVDIVISDCNMPQMGGLEMARTIRR 844
Cdd:PRK09483     2 INVLLVDDHE-----LVR-AGIRriledikGIKVVGEACCGEDAVKWCrTNAVDVVLMDMNMPGIGGLEATRKILR 71
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
779-844 7.44e-03

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 37.10  E-value: 7.44e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2223346070  779 VLVVEDHLPSQYLLVQQVGYLGHRVLAASNgLEGLATWSEHAV-DIVISDCNMPQMGGLEMARTIRR 844
Cdd:cd19928      1 ILVADDDRAIRTVLTQALGRAGYEVRTTGN-AATLWRWVEEGEgDLVITDVVMPDENGLDLIPRIKK 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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