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Conserved domains on  [gi|1172344048|ref|WP_080727322|]
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MULTISPECIES: HlyD family efflux transporter periplasmic adaptor subunit [Sphingomonadaceae]

Protein Classification

HlyD/EmrA/EmrK family protein( domain architecture ID 1001740)

HlyD/EmrA/EmrK family protein belongs to a family of membrane fusion proteins (MFPs) from proteobacteria that includes the multidrug resistance protein MdtN and the efflux pump membrane proteins EmrA and EmrK

Gene Ontology:  GO:0055085
PubMed:  12501312|12482849

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CusB_dom_1 super family cl46872
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
17-388 7.07e-115

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


The actual alignment was detected with superfamily member PRK15136:

Pssm-ID: 481212 [Multi-domain]  Cd Length: 390  Bit Score: 340.13  E-value: 7.07e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  17 EVESADEETARKAKRKKGFTGLVAAVLLLGGGYYAYDYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKR 96
Cdd:PRK15136    6 ETQTPQQPVKKKGKRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  97 GDILLRLDDTDAKLAVARAEAQLALTERKVRGLIATDSGLGAQIASRAAdqaradaqlaaargELDKARIDLQRREALVA 176
Cdd:PRK15136   86 GDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKT--------------ALAQAQSDLNRRVPLGN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 177 SGSVSGDELTTARNAHTTALAnvkAAEAARSQasanrltavgdRDANKALIADTTVENNPEVLAARTALDQARIDLDRTI 256
Cdd:PRK15136  152 ANLIGREELQHARDAVASAQA---QLDVAIQQ-----------YNANQAMILNTPLEDQPAVQQAATEVRNAWLALQRTK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVEYKGKVIGFSGGTG 336
Cdd:PRK15136  218 IVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYGDDVVYTGKVVGLDMGTG 297
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1172344048 337 SAFAVVPAQNATGNWIKVVQRLPVRIALDPKQLAEHPLQVGLSMTADIDLSN 388
Cdd:PRK15136  298 SAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIGLSTLVTVDTAN 349
 
Name Accession Description Interval E-value
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
17-388 7.07e-115

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 340.13  E-value: 7.07e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  17 EVESADEETARKAKRKKGFTGLVAAVLLLGGGYYAYDYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKR 96
Cdd:PRK15136    6 ETQTPQQPVKKKGKRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  97 GDILLRLDDTDAKLAVARAEAQLALTERKVRGLIATDSGLGAQIASRAAdqaradaqlaaargELDKARIDLQRREALVA 176
Cdd:PRK15136   86 GDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKT--------------ALAQAQSDLNRRVPLGN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 177 SGSVSGDELTTARNAHTTALAnvkAAEAARSQasanrltavgdRDANKALIADTTVENNPEVLAARTALDQARIDLDRTI 256
Cdd:PRK15136  152 ANLIGREELQHARDAVASAQA---QLDVAIQQ-----------YNANQAMILNTPLEDQPAVQQAATEVRNAWLALQRTK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVEYKGKVIGFSGGTG 336
Cdd:PRK15136  218 IVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYGDDVVYTGKVVGLDMGTG 297
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1172344048 337 SAFAVVPAQNATGNWIKVVQRLPVRIALDPKQLAEHPLQVGLSMTADIDLSN 388
Cdd:PRK15136  298 SAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIGLSTLVTVDTAN 349
8a0101 TIGR00998
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ...
31-384 1.97e-113

efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]


Pssm-ID: 273385 [Multi-domain]  Cd Length: 334  Bit Score: 334.46  E-value: 1.97e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  31 RKKGFTGLVAAVLLLGGGYYAYDYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKL 110
Cdd:TIGR00998   1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 111 AVARAEAQLALTERKVRGLIATDSGLGAQIASRAADQARADaqlaaarGELDKARIDLQRREALVASGSVSGDELTTARN 190
Cdd:TIGR00998  81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQAR-------EKLLQAELDLRRRVPLFKKGLISREELDHARK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 191 AHTTALANVkaaEAARSQASAnrltavgdrdANKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSKRQV 270
Cdd:TIGR00998 154 ALLSAKAAL---NAAIQEQLN----------ANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFV 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 271 QVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVEYKGKVIGFSGGTGSAFAVVPAQNATGN 350
Cdd:TIGR00998 221 QVGQVVSPGQPLMAVVPAEQMYVEANFKETQLKNVRIGQPVTIRSDLYGSDVVFEGKVTGISMGTGSAFSLLPAQNATGN 300
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1172344048 351 WIKVVQRLPVRIALDPKQLAEHPLQVGLSMTADI 384
Cdd:TIGR00998 301 WIKVVQRLPVRIKLDPKELDEHPLRIGLSAEVEI 334
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
28-386 7.46e-76

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 238.02  E-value: 7.46e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  28 KAKRKKGFTGLVAAVLLLGGGYYAYdYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTD 107
Cdd:COG1566     2 KALKKRRLLALVLLLLALGLALWAA-GRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 108 AKLAVARAEAQLALTERKVRGLIATdSGLGAQIASRAADQARADAqlaaargELDKARIDLQRREALVASGSVSGDELTT 187
Cdd:COG1566    81 LQAALAQAEAQLAAAEAQLARLEAE-LGAEAEIAAAEAQLAAAQA-------QLDLAQRELERYQALYKKGAVSQQELDE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 188 ARNAHTTALANVKAAEAARSQASAnrltavgdrdanKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSK 267
Cdd:COG1566   153 ARAALDAAQAQLEAAQAQLAQAQA------------GLREEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTN 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 268 RQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDnVEYKGKVIGFSGGTGSAfavVPAQNA 347
Cdd:COG1566   221 LNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPD-RVFEGKVTSISPGAGFT---SPPKNA 296
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1172344048 348 TGNwikVVQRLPVRIALDPKQLaeHPLQVGLSMTADIDL 386
Cdd:COG1566   297 TGN---VVQRYPVRIRLDNPDP--EPLRPGMSATVEIDT 330
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
56-386 4.20e-54

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 181.47  E-value: 4.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  56 VASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTERKV--------- 126
Cdd:pfam00529   4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVarlqaeldr 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 127 -RGLIATDSGLGAQIASRAADQARADAQLAAARGELDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAA 205
Cdd:pfam00529  84 lQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 206 RSQASANrltAVGDRDANKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSKRQVQV-GQRVSSGQTLMV 284
Cdd:pfam00529 164 LDQIYVQ---ITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 285 VVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNV--EYKGKVIGFSGGTGsafavvpaqnatgnwikvvqrlPVRI 362
Cdd:pfam00529 241 VVPEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgRFTGVVVGISPDTG----------------------PVRV 298
                         330       340
                  ....*....|....*....|....
gi 1172344048 363 ALDPKQLAEHPLQVGLSMTADIDL 386
Cdd:pfam00529 299 VVDKAQGPYYPLRIGLSAGALVRL 322
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
255-285 1.86e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 36.63  E-value: 1.86e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1172344048 255 TIIRAPVDGIVSKRQVQVGQRVSSGQTLMVV 285
Cdd:cd06850    37 NEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
 
Name Accession Description Interval E-value
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
17-388 7.07e-115

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 340.13  E-value: 7.07e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  17 EVESADEETARKAKRKKGFTGLVAAVLLLGGGYYAYDYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKR 96
Cdd:PRK15136    6 ETQTPQQPVKKKGKRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  97 GDILLRLDDTDAKLAVARAEAQLALTERKVRGLIATDSGLGAQIASRAAdqaradaqlaaargELDKARIDLQRREALVA 176
Cdd:PRK15136   86 GDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKT--------------ALAQAQSDLNRRVPLGN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 177 SGSVSGDELTTARNAHTTALAnvkAAEAARSQasanrltavgdRDANKALIADTTVENNPEVLAARTALDQARIDLDRTI 256
Cdd:PRK15136  152 ANLIGREELQHARDAVASAQA---QLDVAIQQ-----------YNANQAMILNTPLEDQPAVQQAATEVRNAWLALQRTK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVEYKGKVIGFSGGTG 336
Cdd:PRK15136  218 IVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYGDDVVYTGKVVGLDMGTG 297
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1172344048 337 SAFAVVPAQNATGNWIKVVQRLPVRIALDPKQLAEHPLQVGLSMTADIDLSN 388
Cdd:PRK15136  298 SAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIGLSTLVTVDTAN 349
8a0101 TIGR00998
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ...
31-384 1.97e-113

efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]


Pssm-ID: 273385 [Multi-domain]  Cd Length: 334  Bit Score: 334.46  E-value: 1.97e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  31 RKKGFTGLVAAVLLLGGGYYAYDYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKL 110
Cdd:TIGR00998   1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 111 AVARAEAQLALTERKVRGLIATDSGLGAQIASRAADQARADaqlaaarGELDKARIDLQRREALVASGSVSGDELTTARN 190
Cdd:TIGR00998  81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQAR-------EKLLQAELDLRRRVPLFKKGLISREELDHARK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 191 AHTTALANVkaaEAARSQASAnrltavgdrdANKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSKRQV 270
Cdd:TIGR00998 154 ALLSAKAAL---NAAIQEQLN----------ANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFV 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 271 QVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVEYKGKVIGFSGGTGSAFAVVPAQNATGN 350
Cdd:TIGR00998 221 QVGQVVSPGQPLMAVVPAEQMYVEANFKETQLKNVRIGQPVTIRSDLYGSDVVFEGKVTGISMGTGSAFSLLPAQNATGN 300
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1172344048 351 WIKVVQRLPVRIALDPKQLAEHPLQVGLSMTADI 384
Cdd:TIGR00998 301 WIKVVQRLPVRIKLDPKELDEHPLRIGLSAEVEI 334
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
28-386 7.46e-76

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 238.02  E-value: 7.46e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  28 KAKRKKGFTGLVAAVLLLGGGYYAYdYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTD 107
Cdd:COG1566     2 KALKKRRLLALVLLLLALGLALWAA-GRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 108 AKLAVARAEAQLALTERKVRGLIATdSGLGAQIASRAADQARADAqlaaargELDKARIDLQRREALVASGSVSGDELTT 187
Cdd:COG1566    81 LQAALAQAEAQLAAAEAQLARLEAE-LGAEAEIAAAEAQLAAAQA-------QLDLAQRELERYQALYKKGAVSQQELDE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 188 ARNAHTTALANVKAAEAARSQASAnrltavgdrdanKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSK 267
Cdd:COG1566   153 ARAALDAAQAQLEAAQAQLAQAQA------------GLREEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTN 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 268 RQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDnVEYKGKVIGFSGGTGSAfavVPAQNA 347
Cdd:COG1566   221 LNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPD-RVFEGKVTSISPGAGFT---SPPKNA 296
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1172344048 348 TGNwikVVQRLPVRIALDPKQLaeHPLQVGLSMTADIDL 386
Cdd:COG1566   297 TGN---VVQRYPVRIRLDNPDP--EPLRPGMSATVEIDT 330
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
56-386 4.20e-54

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 181.47  E-value: 4.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  56 VASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTERKV--------- 126
Cdd:pfam00529   4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVarlqaeldr 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 127 -RGLIATDSGLGAQIASRAADQARADAQLAAARGELDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAA 205
Cdd:pfam00529  84 lQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 206 RSQASANrltAVGDRDANKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSKRQVQV-GQRVSSGQTLMV 284
Cdd:pfam00529 164 LDQIYVQ---ITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 285 VVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNV--EYKGKVIGFSGGTGsafavvpaqnatgnwikvvqrlPVRI 362
Cdd:pfam00529 241 VVPEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgRFTGVVVGISPDTG----------------------PVRV 298
                         330       340
                  ....*....|....*....|....
gi 1172344048 363 ALDPKQLAEHPLQVGLSMTADIDL 386
Cdd:pfam00529 299 VVDKAQGPYYPLRIGLSAGALVRL 322
PRK10476 PRK10476
multidrug transporter subunit MdtN;
24-384 1.55e-40

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 146.71  E-value: 1.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  24 ETARKAKRKKGFTGL--VAAVLLLGggyyAYDYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILL 101
Cdd:PRK10476    2 ESTPKKSPRKKLPALaiVALAIVAL----VFVIWRTDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 102 RLDDTDAKLAVARAEAQLALTERKV----RGLIATDSglGAQIASRAADQARADaqlaaargeLDKARIDLQRREALVAS 177
Cdd:PRK10476   78 RIDPRPYELTVAQAQADLALADAQImttqRSVDAERS--NAASANEQVERARAN---------AKLATRTLERLEPLLAK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 178 GSVSGDELTTARNAHTTALANVKAAEAARSQASAnrltAVGDRDANKALIAdttvennpevlAARTALDQARIDLDRTII 257
Cdd:PRK10476  147 GYVSAQQVDQARTAQRDAEVSLNQALLQAQAAAA----AVGGVDALVAQRA-----------AREAALAIAELHLEDTTV 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 258 RAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISdLYGDNVEYKGKVIGFSGGTGS 337
Cdd:PRK10476  212 RAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYS-MIDRGRPFEGKVDSIGWGVLP 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1172344048 338 AFAV-----VPAQNATGNWIKVVQRLPVRIALD--PKQLaehpLQVGLSMTADI 384
Cdd:PRK10476  291 DDGGnvprgLPYVPRSINWVRVAQRFPVRIMLDkpDPEL----FRIGASAVVEL 340
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
71-387 7.27e-34

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 128.14  E-value: 7.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  71 NVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTERkvrgliatdsglgaqiasraadqara 150
Cdd:COG0845    22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQA-------------------------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 151 daqlaaargELDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAArsqasanrltavgdrdankaliadt 230
Cdd:COG0845    76 ---------QLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAA------------------------- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 231 tvennpevlaartaLDQARIDLDRTIIRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQS 310
Cdd:COG0845   122 --------------LEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQP 187
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172344048 311 VTLISDLYGDnVEYKGKVIgfsggtgsafAVVPAQNATgnwikvVQRLPVRIALDPkqlAEHPLQVGLSMTADIDLS 387
Cdd:COG0845   188 VTVTLDAGPG-KTFEGKVT----------FIDPAVDPA------TRTVRVRAELPN---PDGLLRPGMFVRVRIVLG 244
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
32-331 8.10e-24

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 100.81  E-value: 8.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  32 KKGFTGLVAAVLLLGGGYYAYDYFvASRHAVTDNAYVGANVAQVTpL---IGGPVREVLVDDTQKVKRGDILLRLDDT-- 106
Cdd:PRK03598    2 KKKVVIGLAVVVLAAAVAGGWWWY-QSRQDNGLTLYGNVDIRTVN-LgfrVGGRLASLAVDEGDAVKAGQVLGELDAApy 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 107 -----DAKLAVARAEAQLALTERKVRgliatdSGLGAQIASRAADQARadaqlaaargELDKARIDLQRREALVASGSVS 181
Cdd:PRK03598   80 enalmQAKANVSVAQAQLDLMLAGYR------DEEIAQARAAVKQAQA----------AYDYAQNFYNRQQGLWKSRTIS 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 182 GDELTTARNAHTTALANVKAAEAARSQASA-NRltaVGDRDANKAliadttvennpEVLAARTALDQARIDLDRTIIRAP 260
Cdd:PRK03598  144 ANDLENARSSRDQAQATLKSAQDKLSQYREgNR---PQDIAQAKA-----------SLAQAQAALAQAELNLQDTELIAP 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172344048 261 VDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVeYKGKvIGF 331
Cdd:PRK03598  210 SDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKP-YHGQ-IGF 278
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
68-328 8.98e-23

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 97.39  E-value: 8.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  68 VGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTErkvrgliatdsglgAQiasraadq 147
Cdd:TIGR01730  22 EAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAE--------------AQ-------- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 148 aradaqlaaargeLDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAArsqasanrltavgdrdankali 227
Cdd:TIGR01730  80 -------------LELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKAS---------------------- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 228 adttvennpevlaartaLDQARIDLDRTIIRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRP 307
Cdd:TIGR01730 125 -----------------LASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRR 187
                         250       260
                  ....*....|....*....|.
gi 1172344048 308 GQSVTLISDLYgDNVEYKGKV 328
Cdd:TIGR01730 188 GQTLTVELDAL-PGEEFKGKL 207
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
63-373 2.69e-17

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 81.71  E-value: 2.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  63 TDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTERKVrgliatdsglgaqias 142
Cdd:PRK10559   38 TRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLA---------------- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 143 raadqaradaqlaaargelDKARIDLQRREALVASgSVSGDELTTARNAHTTALANVKAAEAARsqasanrltavgdrda 222
Cdd:PRK10559  102 -------------------QEKRREAGRRNRLGVQ-AMSREEIDQANNVLQTVLHQLAKAQATR---------------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 223 nkaliadttvennpevlaartalDQARIDLDRTIIRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQL 302
Cdd:PRK10559  146 -----------------------DLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKL 202
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172344048 303 AKVRPGQSVTlISDLyGDNVEYKGKVIGFSGGTGSAFAVVPAQ-----NATGNWIKVVQRLPVRIALDPKQLAEHP 373
Cdd:PRK10559  203 EGVRPGYRAE-ITPL-GSNKVLKGTVDSVAAGVTNSSSTRDSKgmatiDSNLEWVRLAQRVPVRIRLDNQQGNLYP 276
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
71-384 9.14e-15

type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 130902 [Multi-domain]  Cd Length: 423  Bit Score: 75.43  E-value: 9.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  71 NVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTD----------------AKLAVARAEA----------------- 117
Cdd:TIGR01843  42 NVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDveadaaelesqvlrleAEVARLRAEAdsqaaiefpddllsaed 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 118 ---------QLALTERKVRGLIATDSGLGAQIASRAADQARADAQLAAARGELDKARIDLQRREALVASGSVSGDELTTA 188
Cdd:TIGR01843 122 pavpelikgQQSLFESRKSTLRAQLELILAQIKQLEAELAGLQAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLEL 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 189 ---RNAHTTALANVKA-AEAARSQASANRLTAVGDRDANKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGI 264
Cdd:TIGR01843 202 ereRAEAQGELGRLEAeLEVLKRQIDELQLERQQIEQTFREEVLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGT 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 265 V-SKRQVQVGQRVSSGQTLMVVVPV-QAAYVDANFKEVQLAKVRPGQSVTLISDLYgDNVEY---KGKVIGFSGGTgsaf 339
Cdd:TIGR01843 282 VqSLKVHTVGGVVQPGETLMEIVPEdDPLEIEAKLSPKDIGFVHVGQPAEIKFSAF-PYRRYgilNGKVKSISPDT---- 356
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1172344048 340 avVPAQNATGNWIKVVQRLPVR-IALDPKQLAEHPlqvGLSMTADI 384
Cdd:TIGR01843 357 --FTDERGGGPYYRVRISIDQNtLGIGPKGLELSP---GMPVTADI 397
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
257-337 8.17e-11

HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.


Pssm-ID: 433206 [Multi-domain]  Cd Length: 104  Bit Score: 58.53  E-value: 8.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDnVEYKGKVIGFSGGTG 336
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSD-YTLEGKVVRISPTVD 80

                  .
gi 1172344048 337 S 337
Cdd:pfam13437  81 P 81
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
70-297 1.03e-10

MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 62.89  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  70 ANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTErkvrgliATdsglgaqiasraadqar 149
Cdd:PRK11556   85 ANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQ-------AT----------------- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 150 adaqlaaargeLDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAArsqasanrltavgdrdankaliad 229
Cdd:PRK11556  141 -----------LANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEAS------------------------ 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172344048 230 ttvennpevlaartaLDQARIDLDRTIIRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANF 297
Cdd:PRK11556  186 ---------------VASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVF 238
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
184-329 5.27e-10

Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.


Pssm-ID: 435440 [Multi-domain]  Cd Length: 214  Bit Score: 58.67  E-value: 5.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 184 ELTTARNAHTTALANVKA-AEAARSQASANRLTAVGdrdANKALIAdttvennpevlaartALDQARIDLDRTIIRAPVD 262
Cdd:pfam16576  55 ELVAAQQEYLLALRSGDAlSKSELLRAARQRLRLLG---MPEAQIA---------------ELERTGKVQPTVTVYAPIS 116
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172344048 263 GIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVeYKGKVI 329
Cdd:pfam16576 117 GVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKT-FEGKVD 182
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
71-120 2.90e-08

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 49.36  E-value: 2.90e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1172344048  71 NVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLA 120
Cdd:pfam13533   1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
185-280 3.84e-04

MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 42.09  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 185 LTTARNAHTTALANVKAAEAA-----RSQASANRLTAVGDRDANKALIADTTVEnnPEVLAARTALDQARIDLDRTIIRA 259
Cdd:PRK09578   99 LKAARDAAAGALAKAEAAHLAaldkrRRYDDLVRDRAVSERDYTEAVADERQAK--AAVASAKAELARAQLQLDYATVTA 176
                          90       100
                  ....*....|....*....|.
gi 1172344048 260 PVDGIVSKRQVQVGQRVSSGQ 280
Cdd:PRK09578  177 PIDGRARRALVTEGALVGQDQ 197
PRK09859 PRK09859
multidrug transporter subunit MdtE;
72-289 6.23e-04

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 41.62  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  72 VAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLAlterkvrgliatdsglGAQIASraadqarad 151
Cdd:PRK09859   61 VAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLA----------------KALSTA--------- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 152 aqlaaargelDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAARSQASANRLTA------VGDRDANKA 225
Cdd:PRK09859  116 ----------SNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYAnvtspiTGVSGKSSV 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172344048 226 LIADTTVENNPEVLAARTALDQARIDLDRTIirapvdgivsKRQVQVGQRVSSGQTLMV--VVPVQ 289
Cdd:PRK09859  186 TVGALVTANQADSLVTVQRLDPIYVDLTQSV----------QDFLRMKEEVASGQIKQVqgSTPVQ 241
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
68-309 7.69e-04

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 41.30  E-value: 7.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048  68 VGANVAqvtpligGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLalterkvrgliatdSGLGAQIASRAAdq 147
Cdd:PRK11578   64 VGAQVS-------GQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATL--------------MELRAQRQQAEA-- 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 148 aradaqlaaargELDKARIDLQRREALVASGSVSGDELTTARnahtTALAnVKAAEAARSQASANRltavgdrdaNKAli 227
Cdd:PRK11578  121 ------------ELKLARVTLSRQQRLAKTQAVSQQDLDTAA----TELA-VKQAQIGTIDAQIKR---------NQA-- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 228 adttvennpevlaartALDQARIDLDRTIIRAPVDGIVSKRQVQVGQRVSSGQ---TLMVVVPVQAAYVDANFKEVQLAK 304
Cdd:PRK11578  173 ----------------SLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQqapNILTLADMSTMLVKAQVSEADVIH 236

                  ....*
gi 1172344048 305 VRPGQ 309
Cdd:PRK11578  237 LKPGQ 241
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
187-294 1.46e-03

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 40.47  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 187 TARNAHTTALANVKAAEAARS--QASANRLTA------VGDRDANKALiADTTvENNPEVLAARTALDQARIDLDRTIIR 258
Cdd:PRK15030  100 TYQATYDSAKGDLAKAQAAANiaQLTVNRYQKllgtqyISKQEYDQAL-ADAQ-QANAAVTAAKAAVETARINLAYTKVT 177
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1172344048 259 APVDGIVSKRQVQVGQRVSSGQ--TLMVVVPVQAAYVD 294
Cdd:PRK15030  178 SPISGRIGKSNVTEGALVQNGQatALATVQQLDPIYVD 215
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
255-285 1.86e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 36.63  E-value: 1.86e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1172344048 255 TIIRAPVDGIVSKRQVQVGQRVSSGQTLMVV 285
Cdd:cd06850    37 NEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
257-312 1.94e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 36.24  E-value: 1.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVV------VPVQAAyVDANFKEVqlaKVRPGQSVT 312
Cdd:cd06850     2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLeamkmeNEVTAP-VAGVVKEI---LVKEGDQVE 59
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
257-287 2.88e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 39.83  E-value: 2.88e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVVVP 287
Cdd:PRK09282  562 IQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
257-285 7.52e-03

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 36.41  E-value: 7.52e-03
                          10        20
                  ....*....|....*....|....*....
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVV 285
Cdd:COG0511   107 IEAPVSGTVVEILVENGQPVEYGQPLFVI 135
 
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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