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Conserved domains on  [gi|1816047931|ref|WP_163190040|]
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rhomboid protease YqgP [Bacillus subtilis]

Protein Classification

rhomboid family intramembrane serine protease( domain architecture ID 12026096)

rhomboid family intramembrane serine protease is a membrane-bound protein that catalyzes regulated intramembrane proteolysis, resulting in the release of functional polypeptides from their membrane anchors

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 175-359 5.49e-49

Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 166.96  E-value: 5.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 175 GKPIFTYLFIALQILMFFLLEINGGStntetLVAFGAKENSLIAQGEWWRLLTPIVLHIGIAHLAFNTLALWSVGTAVER 254
Cdd:COG0705     1 RLPPVTLALIALNVLVFLLQLLLGGE-----LLNWLALVPARLLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPLLER 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 255 MYGSGRFLLIYLAAGITGSIASFVFSP---YPSAGASGAIFGCLGALLYVALsNRKMFLRTIGTNIIVIIIINLGFGFA- 330
Cdd:COG0705    76 RLGSKRFLLLYLLSGLGGGLLQLLFSPgsgYPLVGASGAIFGLLGALLVLGP-RRRVLLLFIPIPALLFLLVWLLLGLLf 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1816047931 331 ----VSNIDNSGHIGGLIGGFFAAAALGLPKAR 359
Cdd:COG0705   155 gllgGGGIAWEAHLGGLLAGLLLALLLRKLRRR 187
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 389-490 2.31e-12

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 64.44  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 389 QESALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLY 468
Cdd:COG4783     3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82

                          90       100
                  ....*....|....*....|..
gi 1816047931 469 AEKNELAQAEKAIRTAVKLKPK 490
Cdd:COG4783    83 LKAGDYDEALALLEKALKLDPE 104
 
Name Accession Description Interval E-value
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 175-359 5.49e-49

Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 166.96  E-value: 5.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 175 GKPIFTYLFIALQILMFFLLEINGGStntetLVAFGAKENSLIAQGEWWRLLTPIVLHIGIAHLAFNTLALWSVGTAVER 254
Cdd:COG0705     1 RLPPVTLALIALNVLVFLLQLLLGGE-----LLNWLALVPARLLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPLLER 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 255 MYGSGRFLLIYLAAGITGSIASFVFSP---YPSAGASGAIFGCLGALLYVALsNRKMFLRTIGTNIIVIIIINLGFGFA- 330
Cdd:COG0705    76 RLGSKRFLLLYLLSGLGGGLLQLLFSPgsgYPLVGASGAIFGLLGALLVLGP-RRRVLLLFIPIPALLFLLVWLLLGLLf 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1816047931 331 ----VSNIDNSGHIGGLIGGFFAAAALGLPKAR 359
Cdd:COG0705   155 gllgGGGIAWEAHLGGLLAGLLLALLLRKLRRR 187
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 216-357 2.44e-44

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


Pssm-ID: 426384  Cd Length: 147  Bit Score: 153.15  E-value: 2.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 216 LIAQGEWWRLLTPIVLHIGIAHLAFNTLALWSVGTAVERMYGSGRFLLIYLAAGITGSIASFVFSPY--PSAGASGAIFG 293
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLstPSVGASGAIFG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816047931 294 CLGALLYVALSNRKMFLRTIGTNIIVIIIINLGFGFAV---SNIDNSGHIGGLIGGFFAAAALGLPK 357
Cdd:pfam01694  81 LLGALLVLGPRNRILLFGLIGALLALLLFILLNLVLGLlpgNGVSNLAHLGGLLVGLLLGFILLRRP 147
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
 121-347 9.84e-20

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 89.14  E-value: 9.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 121 LRDDLQAVFPSFRTEDCSEEHASFENAQMAReRFLSLVLkqeeqrkteaavfqngkPIFTY----LFIALQILMFFLLEI 196
Cdd:PTZ00101   10 YRDDYGENTPFNRAEKYYQSQSSFIQRSKPI-DVLNLIF-----------------PHFTWksfiMAISIIQIIVFIISV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 197 NGGSTNTET-----LVAFGAKENSLIAQGEWWRLLTPIVLHIGIAHLAFNTLALWSVGTAVERMYGSGRFLLIYLAAGIT 271
Cdd:PTZ00101   72 SIKPADFLTpsdslLVTLGANVASRIKQGEIHRLILPIFLHANIFHTFFNVFFQLRMGFTLEKNYGIVKIIILYFLTGIY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 272 GSI--ASFVFSPYpSAGASGAIFGCLG------ALLYVALSNRKMFLrtIGTNIIVIIIINLGFGFAVSNIDNSGHIGGL 343
Cdd:PTZ00101  152 GNIlsSSVTYCPI-KVGASTSGMGLLGivtselILLWHVIRHRERVV--FNIIFFSLISFFYYFTFNGSNIDHVGHLGGL 228


                  ....
gi 1816047931 344 IGGF 347
Cdd:PTZ00101  229 LSGI 232
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 389-490 2.31e-12

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 64.44  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 389 QESALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLY 468
Cdd:COG4783     3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82

                          90       100
                  ....*....|....*....|..
gi 1816047931 469 AEKNELAQAEKAIRTAVKLKPK 490
Cdd:COG4783    83 LKAGDYDEALALLEKALKLDPE 104
rhom_GG_sort TIGR03902
rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like ...
 215-310 3.73e-12

rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like intramembrane serine protease. Its species distribution closely matches model TIGR03501, GlyGly-CTERM, which describes a protein targeting domain analogous to LPXTG and PEP-CTERM. In a number of species (Ralstonia eutropha ,R. metallidurans, R. solanacearum, Marinobacter aquaeolei, etc) with just one GlyGly-CTERM protein (i.e., a dedicated system), the rhombosortase and GlyGly-CTERM genes are adjacent.


Pssm-ID: 274845  Cd Length: 154  Bit Score: 64.13  E-value: 3.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 215 SLIAQGEWWRLLTPIVLHIGIAHLAFNTLALWSVGTAVERMYGSGRFLLIYLAAGITGSIASFVFSP----YpsAGASGA 290
Cdd:TIGR03902   9 AAILDGEWWRLLTGHFVHLNWWHLLMNLAGLLLLWALFGRHLRARRLLLLLLLLSLLISLGLLLFLPslqwY--VGLSGV 86

                          90       100
                  ....*....|....*....|..
gi 1816047931 291 IFG--CLGALLYVALSNRKMFL 310
Cdd:TIGR03902  87 LHGlfAWGALRDIRYGRRSGWL 108
TPR_19 pfam14559
Tetratricopeptide repeat;
438-501 1.72e-08

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 51.05  E-value: 1.72e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816047931 438 GEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPKEQRYKELQRQI 501
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAKL 65
LcrH_SycD TIGR02552
type III secretion low calcium response chaperone LcrH/SycD; Genes in this family are found in ...
 396-507 1.54e-07

type III secretion low calcium response chaperone LcrH/SycD; Genes in this family are found in type III secretion operons. LcrH, from Yersinia is believed to have a regulatory function in the low-calcium response of the secretion system. The same protein is also known as SycD (SYC = Specific Yop Chaperone) for its chaperone role. In Pseudomonas, where the homolog is known as PcrH, the chaperone role has been demonstrated and the regulatory role appears to be absent. ScyD/LcrH contains three central tetratricopeptide-like repeats that are predicted to fold into an all-alpha-helical array.


Pssm-ID: 274197 [Multi-domain]  Cd Length: 135  Bit Score: 50.37  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 396 QASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELA 475
Cdd:TIGR02552  23 LAYNLYQQGRYDEALKLFQLLAAYDPYNSRYWLGLAACCQMLKEYEEAIDAYALAAALDPDDPRPYFHAAECLLALGEPE 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1816047931 476 QAEKAIRTAVKLKPKEQRYKELQRQIENNKES 507
Cdd:TIGR02552 103 SALKALDLAIEICGENPEYSELKERAEAMLES 134
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 391-481 3.89e-04

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 42.62  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 391 SALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKD-HASYYNLALLYA 469
Cdd:cd24142     1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDGgYEKYLYLGQLSG 80

                          90
                  ....*....|..
gi 1816047931 470 EKNELAQAEKAI 481
Cdd:cd24142    81 GEEALQYYEKGI 92
 
Name Accession Description Interval E-value
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 175-359 5.49e-49

Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 166.96  E-value: 5.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 175 GKPIFTYLFIALQILMFFLLEINGGStntetLVAFGAKENSLIAQGEWWRLLTPIVLHIGIAHLAFNTLALWSVGTAVER 254
Cdd:COG0705     1 RLPPVTLALIALNVLVFLLQLLLGGE-----LLNWLALVPARLLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPLLER 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 255 MYGSGRFLLIYLAAGITGSIASFVFSP---YPSAGASGAIFGCLGALLYVALsNRKMFLRTIGTNIIVIIIINLGFGFA- 330
Cdd:COG0705    76 RLGSKRFLLLYLLSGLGGGLLQLLFSPgsgYPLVGASGAIFGLLGALLVLGP-RRRVLLLFIPIPALLFLLVWLLLGLLf 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1816047931 331 ----VSNIDNSGHIGGLIGGFFAAAALGLPKAR 359
Cdd:COG0705   155 gllgGGGIAWEAHLGGLLAGLLLALLLRKLRRR 187
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 216-357 2.44e-44

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


Pssm-ID: 426384  Cd Length: 147  Bit Score: 153.15  E-value: 2.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 216 LIAQGEWWRLLTPIVLHIGIAHLAFNTLALWSVGTAVERMYGSGRFLLIYLAAGITGSIASFVFSPY--PSAGASGAIFG 293
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLstPSVGASGAIFG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816047931 294 CLGALLYVALSNRKMFLRTIGTNIIVIIIINLGFGFAV---SNIDNSGHIGGLIGGFFAAAALGLPK 357
Cdd:pfam01694  81 LLGALLVLGPRNRILLFGLIGALLALLLFILLNLVLGLlpgNGVSNLAHLGGLLVGLLLGFILLRRP 147
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
 121-347 9.84e-20

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 89.14  E-value: 9.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 121 LRDDLQAVFPSFRTEDCSEEHASFENAQMAReRFLSLVLkqeeqrkteaavfqngkPIFTY----LFIALQILMFFLLEI 196
Cdd:PTZ00101   10 YRDDYGENTPFNRAEKYYQSQSSFIQRSKPI-DVLNLIF-----------------PHFTWksfiMAISIIQIIVFIISV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 197 NGGSTNTET-----LVAFGAKENSLIAQGEWWRLLTPIVLHIGIAHLAFNTLALWSVGTAVERMYGSGRFLLIYLAAGIT 271
Cdd:PTZ00101   72 SIKPADFLTpsdslLVTLGANVASRIKQGEIHRLILPIFLHANIFHTFFNVFFQLRMGFTLEKNYGIVKIIILYFLTGIY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 272 GSI--ASFVFSPYpSAGASGAIFGCLG------ALLYVALSNRKMFLrtIGTNIIVIIIINLGFGFAVSNIDNSGHIGGL 343
Cdd:PTZ00101  152 GNIlsSSVTYCPI-KVGASTSGMGLLGivtselILLWHVIRHRERVV--FNIIFFSLISFFYYFTFNGSNIDHVGHLGGL 228


                  ....
gi 1816047931 344 IGGF 347
Cdd:PTZ00101  229 LSGI 232
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 389-490 2.31e-12

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 64.44  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 389 QESALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLY 468
Cdd:COG4783     3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82

                          90       100
                  ....*....|....*....|..
gi 1816047931 469 AEKNELAQAEKAIRTAVKLKPK 490
Cdd:COG4783    83 LKAGDYDEALALLEKALKLDPE 104
rhom_GG_sort TIGR03902
rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like ...
 215-310 3.73e-12

rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like intramembrane serine protease. Its species distribution closely matches model TIGR03501, GlyGly-CTERM, which describes a protein targeting domain analogous to LPXTG and PEP-CTERM. In a number of species (Ralstonia eutropha ,R. metallidurans, R. solanacearum, Marinobacter aquaeolei, etc) with just one GlyGly-CTERM protein (i.e., a dedicated system), the rhombosortase and GlyGly-CTERM genes are adjacent.


Pssm-ID: 274845  Cd Length: 154  Bit Score: 64.13  E-value: 3.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 215 SLIAQGEWWRLLTPIVLHIGIAHLAFNTLALWSVGTAVERMYGSGRFLLIYLAAGITGSIASFVFSP----YpsAGASGA 290
Cdd:TIGR03902   9 AAILDGEWWRLLTGHFVHLNWWHLLMNLAGLLLLWALFGRHLRARRLLLLLLLLSLLISLGLLLFLPslqwY--VGLSGV 86

                          90       100
                  ....*....|....*....|..
gi 1816047931 291 IFG--CLGALLYVALSNRKMFL 310
Cdd:TIGR03902  87 LHGlfAWGALRDIRYGRRSGWL 108
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 392-502 1.52e-10

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 58.86  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 392 ALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEK 471
Cdd:COG4235    19 GWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQ 98

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1816047931 472 NELAQAEKAIRTAVKLKPKEQRYKELQRQIE 502
Cdd:COG4235    99 GDYAEAIAAWQKLLALLPADAPARLLEASIA 129
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 349-489 2.01e-10

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 63.09  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 349 AAAALGLPKARAFGKRVLSAVLLIALAAGFLYYGLHSPSHQESALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLK 428
Cdd:COG3914    37 LAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALF 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816047931 429 ILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKP 489
Cdd:COG3914   117 NLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDP 177
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 383-490 2.34e-10

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 61.28  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 383 LHSPSHQESALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYY 462
Cdd:COG2956   103 LELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALL 182

                          90       100
                  ....*....|....*....|....*...
gi 1816047931 463 NLALLYAEKNELAQAEKAIRTAVKLKPK 490
Cdd:COG2956   183 LLAELYLEQGDYEEAIAALERALEQDPD 210
PRK10907 PRK10907
intramembrane serine protease GlpG; Provisional
 179-300 1.57e-09

intramembrane serine protease GlpG; Provisional


Pssm-ID: 182828 [Multi-domain]  Cd Length: 276  Bit Score: 58.86  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 179 FTYLFIALQILMFFLLEINGGSTnTETLVAFGAkENSLiaQGEWWRLLTPIVLHIGIAHLAFNTLALWSVGTAVERMYGS 258
Cdd:PRK10907   96 LTLGVMIACVVVFILMQILGDQT-VMLWLAWPF-DPSL--KFELWRYFTHALLHFSLLHILFNLLWWWYLGGAVEKRLGS 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1816047931 259 GRFLLIylaagitgSIASFVFSPYPSAGASGAIFGCLGALLY 300
Cdd:PRK10907  172 GKLIVI--------TLISALLSGWVQSKFSGPWFGGLSGVVY 205
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 347-489 1.72e-09

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 56.51  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 347 FFAAAALGLPKARAFGKRVLSAVLLIALAAGFLYYGLHSPSHQESALIQQASELYQEGKYEEVTELLNGEAAQKDASADL 426
Cdd:COG5010    11 PLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPEL 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816047931 427 LKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKP 489
Cdd:COG5010    91 YYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
392-490 2.96e-09

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.71  E-value: 2.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 392 ALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEK 471
Cdd:COG0457    10 AYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQAL 89

                          90
                  ....*....|....*....
gi 1816047931 472 NELAQAEKAIRTAVKLKPK 490
Cdd:COG0457    90 GRYEEALEDYDKALELDPD 108
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 392-491 3.66e-09

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 55.20  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 392 ALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEK 471
Cdd:COG4783    40 AFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRAL 119

                          90       100
                  ....*....|....*....|
gi 1816047931 472 NELAQAEKAIRTAVKLKPKE 491
Cdd:COG4783   120 GRPDEAIAALEKALELDPDD 139
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 392-502 5.64e-09

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 57.05  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 392 ALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEK 471
Cdd:COG2956    78 ALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQ 157

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1816047931 472 NELAQAEKAIRTAVKLKPKEQRYKELQRQIE 502
Cdd:COG2956   158 GDYDEAIEALEKALKLDPDCARALLLLAELY 188
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 370-501 1.51e-08

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 55.89  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 370 LLIALAAGFLYYglhspshqesaliQQASELYQEGKYEEVTELLNgEAAQKDA-SADLLKILAVSDIQIGEYDQAVSLLE 448
Cdd:COG2956     1 LLLPVAAALGWY-------------FKGLNYLLNGQPDKAIDLLE-EALELDPeTVEAHLALGNLYRRRGEYDRAIRIHQ 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1816047931 449 RAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPKEQRYKELQRQI 501
Cdd:COG2956    67 KLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEI 119
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 384-494 1.70e-08

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 56.93  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 384 HSPSHQEsALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYN 463
Cdd:COG3914   107 LNPDNAE-ALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNN 185

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1816047931 464 LALLYAEKNELAQAEKAIRTAVKLKPKEQRY 494
Cdd:COG3914   186 LGNALQDLGRLEEAIAAYRRALELDPDNADA 216
TPR_19 pfam14559
Tetratricopeptide repeat;
438-501 1.72e-08

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 51.05  E-value: 1.72e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816047931 438 GEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPKEQRYKELQRQI 501
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAKL 65
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 348-489 1.76e-08

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 56.93  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 348 FAAAALGLPKARAFGKRVLSAVLLIALAAGFLYYGLHSPSHQESALIQQASELYQEGKYEEVTELLNGEAAQKDASADLL 427
Cdd:COG3914     7 LALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAAL 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816047931 428 KILavsdiQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKP 489
Cdd:COG3914    87 LLQ-----ALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNP 143
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
392-490 1.99e-08

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 55.01  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 392 ALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEK 471
Cdd:COG0457    44 ALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLEL 123

                          90
                  ....*....|....*....
gi 1816047931 472 NELAQAEKAIRTAVKLKPK 490
Cdd:COG0457   124 GRYDEAIEAYERALELDPD 142
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 421-491 4.66e-08

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 52.12  E-value: 4.66e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816047931 421 DASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPKE 491
Cdd:COG4783     1 AACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDE 71
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
400-493 4.88e-08

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 50.55  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 400 LYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLlERAVKKEPKDHASYYNLALLYAEKNELAQAEK 479
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNLAELLLELGDYDEALA 80

                          90
                  ....*....|....
gi 1816047931 480 AIRTAVKLKPKEQR 493
Cdd:COG3063    81 YLERALELDPSALR 94
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 373-493 5.07e-08

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 52.27  E-value: 5.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 373 ALAAGFLYYGLHSPSHQESALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVK 452
Cdd:COG5010     3 ALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQ 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1816047931 453 KEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPKEQR 493
Cdd:COG5010    83 LDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPN 123
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 387-506 1.44e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 52.81  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 387 SHQESALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLAL 466
Cdd:COG2956    39 PETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAE 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1816047931 467 LYAEKNELAQAEKAIRTAVKLKPKE-QRYKELQRQIENNKE 506
Cdd:COG2956   119 IYEQEGDWEKAIEVLERLLKLGPENaHAYCELAELYLEQGD 159
LcrH_SycD TIGR02552
type III secretion low calcium response chaperone LcrH/SycD; Genes in this family are found in ...
 396-507 1.54e-07

type III secretion low calcium response chaperone LcrH/SycD; Genes in this family are found in type III secretion operons. LcrH, from Yersinia is believed to have a regulatory function in the low-calcium response of the secretion system. The same protein is also known as SycD (SYC = Specific Yop Chaperone) for its chaperone role. In Pseudomonas, where the homolog is known as PcrH, the chaperone role has been demonstrated and the regulatory role appears to be absent. ScyD/LcrH contains three central tetratricopeptide-like repeats that are predicted to fold into an all-alpha-helical array.


Pssm-ID: 274197 [Multi-domain]  Cd Length: 135  Bit Score: 50.37  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 396 QASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELA 475
Cdd:TIGR02552  23 LAYNLYQQGRYDEALKLFQLLAAYDPYNSRYWLGLAACCQMLKEYEEAIDAYALAAALDPDDPRPYFHAAECLLALGEPE 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1816047931 476 QAEKAIRTAVKLKPKEQRYKELQRQIENNKES 507
Cdd:TIGR02552 103 SALKALDLAIEICGENPEYSELKERAEAMLES 134
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 392-502 4.99e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 51.27  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 392 ALIQQASELYQEGKYEEVTELLNgEAAQKD-ASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAE 470
Cdd:COG2956   146 AYCELAELYLEQGDYDEAIEALE-KALKLDpDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEK 224

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1816047931 471 KNELAQAEKAIRTAVKLKPKEQRYKELQRQIE 502
Cdd:COG2956   225 LGDPEEALELLRKALELDPSDDLLLALADLLE 256
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
424-490 5.13e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.78  E-value: 5.13e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816047931 424 ADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPK 490
Cdd:COG0457     8 AEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPD 74
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
392-504 1.46e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 49.62  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 392 ALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEK 471
Cdd:COG0457    78 ALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKL 157

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1816047931 472 NELAQAEKAIRTAVKLKPKEQRYKELQRQIENN 504
Cdd:COG0457   158 GRYEEALELLEKLEAAALAALLAAALGEAALAL 190
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 442-490 7.30e-06

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 45.38  E-value: 7.30e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1816047931 442 QAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPK 490
Cdd:COG4235     1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPD 49
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 392-486 1.24e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 47.03  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 392 ALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHAsYYNLALLYAEK 471
Cdd:COG2956   180 ALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDL-LLALADLLERK 258

                          90
                  ....*....|....*
gi 1816047931 472 NELAQAEKAIRTAVK 486
Cdd:COG2956   259 EGLEAALALLERQLR 273
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 399-503 1.81e-05

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 43.83  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 399 ELYQEGKYEEVTELLN---GEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDH---ASYYNLALLYAEKN 472
Cdd:COG1729     2 ALLKAGDYDEAIAAFKaflKRYPNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPkapDALLKLGLSYLELG 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1816047931 473 ELAQAEKAIRTAVKLKPKEQRYKELQRQIEN 503
Cdd:COG1729    82 DYDKARATLEELIKKYPDSEAAKEARARLAR 112
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
368-490 2.54e-05

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 45.68  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 368 AVLLIALAAGFLYYGLHSPSHQE----SALIQQASELYQEGKYEEVTELLNgEAAQKD-ASADLLKILAVSDIQIGEYDQ 442
Cdd:COG4785    47 ALAAAALAAAALAAERIDRALALpdlaQLYYERGVAYDSLGDYDLAIADFD-QALELDpDLAEAYNNRGLAYLLLGDYDA 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1816047931 443 AVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPK 490
Cdd:COG4785   126 ALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDPN 173
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
352-490 3.87e-05

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 44.91  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 352 ALGLPKARAFGKRVLSAVLLIALAAGFLYYGLHSPSHQESALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILA 431
Cdd:COG4785     1 LYALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQLYYERG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1816047931 432 VSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPK 490
Cdd:COG4785    81 VAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPD 139
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 411-506 8.94e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 45.46  E-value: 8.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 411 ELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPK 490
Cdd:TIGR02917 588 AILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALELKPD 667

                          90
                  ....*....|....*.
gi 1816047931 491 EQRYKELQRQIENNKE 506
Cdd:TIGR02917 668 NTEAQIGLAQLLLAAK 683
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 391-497 1.29e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 44.69  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 391 SALIQQASELYQEGKYEEVTELLngEAAQKDASADLLKILAVSDIQI--GEYDQAVSLLERAVKKEPKDHASYYNLALLY 468
Cdd:TIGR02917 500 PAAANLARIDIQEGNPDDAIQRF--EKVLTIDPKNLRAILALAGLYLrtGNEEEAVAWLEKAAELNPQEIEPALALAQYY 577

                          90       100
                  ....*....|....*....|....*....
gi 1816047931 469 AEKNELAQAEKAIRTAVKLKPKEQRYKEL 497
Cdd:TIGR02917 578 LGKGQLKKALAILNEAADAAPDSPEAWLM 606
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 430-491 1.40e-04

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 40.01  E-value: 1.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816047931 430 LAVSDIQIGEYDQAVSLLERAVKKE---PKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPKE 491
Cdd:pfam13432   3 LARAALRAGDYDDAAAALEAALARFpesPDAAAALLLLGLAALRQGRLAEAAAAYRAALRAAPGD 67
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 400-479 1.92e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 44.30  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 400 LYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEK 479
Cdd:TIGR02917 813 LYLELKDPRALEYAERALKLAPNIPAILDTLGWLLVEKGEADRALPLLRKAVNIAPEAAAIRYHLALALLATGRKAEARK 892
TPR_17 pfam13431
Tetratricopeptide repeat;
446-479 2.56e-04

Tetratricopeptide repeat;


Pssm-ID: 433201 [Multi-domain]  Cd Length: 34  Bit Score: 38.29  E-value: 2.56e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1816047931 446 LLERAVKKEPKDHASYYNLALLYAEKNELAQAEK 479
Cdd:pfam13431   1 LYLKALELDPNNADAYYNLAVLLLELGQSETALQ 34
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 388-497 3.01e-04

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 42.98  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 388 HQESALIQQASELYQEGKYEEVTELLnGEAAQKDASADLLKILAvsDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALL 467
Cdd:COG3071   191 RDPELAAAYARALIALGDHDEAERLL-REALKRQWDPRLVRLYG--RLQGGDPAKQLKRAEKWLKKHPNDPDLLLALGRL 267

                          90       100       110
                  ....*....|....*....|....*....|
gi 1816047931 468 YAEKNELAQAEKAIRTAVKLKPKEQRYKEL 497
Cdd:COG3071   268 CLRNQLWGKAREYLEAALALRPSAEAYAEL 297
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 397-490 3.89e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 43.15  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 397 ASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQ 476
Cdd:TIGR02917 336 ASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGISKLSQGDPSE 415

                          90
                  ....*....|....
gi 1816047931 477 AEKAIRTAVKLKPK 490
Cdd:TIGR02917 416 AIADLETAAQLDPE 429
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 391-481 3.89e-04

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 42.62  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 391 SALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKD-HASYYNLALLYA 469
Cdd:cd24142     1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDGgYEKYLYLGQLSG 80

                          90
                  ....*....|..
gi 1816047931 470 EKNELAQAEKAI 481
Cdd:cd24142    81 GEEALQYYEKGI 92
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 425-491 1.12e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 41.07  E-value: 1.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816047931 425 DLLKILAVSDIQIGEYDQAVSLLERAVKKEPkDHASYYN-LALLYAEKNELAQAEKAIRTAVKLKPKE 491
Cdd:cd24142     1 DELLEKAEELLDQGNFELALKFLQRALELEP-NNVEALElLGEILLELGDVEEAREVLLRAIELDPDG 67
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 416-490 1.34e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.61  E-value: 1.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816047931 416 EAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKPK 490
Cdd:TIGR02917 728 KALKRAPSSQNAIKLHRALLASGNTAEAVKTLEAWLKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPD 802
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 417-492 1.47e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.22  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816047931 417 AAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLK-PKEQ 492
Cdd:TIGR02917  15 SACGDQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFLLGKIYLALGDYAAAEKELRKALSLGyPKNQ 91
TauE pfam01925
Sulfite exporter TauE/SafE; This is a family of integral membrane proteins where the alignment ...
 225-383 1.98e-03

Sulfite exporter TauE/SafE; This is a family of integral membrane proteins where the alignment appears to contain two duplicated modules of three transmembrane helices. The proteins are involved in the transport of anions across the cytoplasmic membrane during taurine metabolism as an exporter of sulfoacetate. This family used to be known as DUF81.


Pssm-ID: 460386  Cd Length: 235  Bit Score: 39.87  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 225 LLTPIVLHIGIAHLAFNTLALWSVGTAVERMYGSGRFLLIYLAAGITGSIASFVFSPYPSAGASGAIFGCLgaLLYVA-- 302
Cdd:pfam01925  28 LLLPPAVAVGTSLLAAVATSLSGALAHRRRGAVDWRLLLRLLLGGLIGALLGALLLLLLPEALLKLLFGVL--LLLAAll 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 303 -LSNRKMFLRTIGTNIIVIIIINLGFGFAVsnidnsGHIGGLIG---GFFAAAAL----GLPKARAFG-KRVLSAVLLIA 373
Cdd:pfam01925 106 mLLRRRLGAAPRARRRRPGPLALALLGGLI------GFLSGLFGiggGFLLVPALlyllGLPLKKAVGtSLLLFLVSNLA 179

                         170
                  ....*....|
gi 1816047931 374 LAAGFLYYGL 383
Cdd:pfam01925 180 ALLGYALLGA 189
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 391-502 2.24e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.84  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 391 SALIQQASELYQEGKYEEVTELLNgEAAQKDAS-ADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYA 469
Cdd:TIGR02917 160 YAKLGLAQLALAENRFDEARALID-EVLTADPGnVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATILI 238

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1816047931 470 EKNELAQAEKAIRTAVKLKPKEQRYKELQRQIE 502
Cdd:TIGR02917 239 EAGEFEEAEKHADALLKKAPNSPLAHYLKALVD 271
TPR_19 pfam14559
Tetratricopeptide repeat;
403-467 2.98e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 36.02  E-value: 2.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816047931 403 EGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALL 467
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAKL 65
TPR_8 pfam13181
Tetratricopeptide repeat;
460-490 3.09e-03

Tetratricopeptide repeat;


Pssm-ID: 404131 [Multi-domain]  Cd Length: 33  Bit Score: 35.07  E-value: 3.09e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1816047931 460 SYYNLALLYAEKNELAQAEKAIRTAVKLKPK 490
Cdd:pfam13181   3 AYYNLGLIYLKLGDYEEAKEYYEKALELDPD 33
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 386-490 4.05e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.07  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 386 PSHQESALIQQASElYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLA 465
Cdd:TIGR02917 292 PEYLPALLLAGASE-YQLGNLEQAYQYLNQILKYAPNSHQARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLG 370

                          90       100
                  ....*....|....*....|....*
gi 1816047931 466 LLYAEKNELAQAEKAIRTAVKLKPK 490
Cdd:TIGR02917 371 EAYLALGDFEKAAEYLAKATELDPE 395
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 389-489 4.38e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 39.68  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 389 QESALIQQASELY-QEGKYEEVTELLN--GEAAQKDASADLLK--------------------------------ILAVS 433
Cdd:TIGR02917 361 DDPAALSLLGEAYlALGDFEKAAEYLAkaTELDPENAAARTQLgisklsqgdpseaiadletaaqldpelgradlLLILS 440

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1816047931 434 DIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIRTAVKLKP 489
Cdd:TIGR02917 441 YLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEP 496
Coatomer_E pfam04733
Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, ...
 394-464 4.57e-03

Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, which is involved in the regulation of intracellular protein trafficking between the endoplasmic reticulum and the Golgi complex.


Pssm-ID: 398419 [Multi-domain]  Cd Length: 288  Bit Score: 39.00  E-value: 4.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816047931 394 IQQASELYQE--GKYEEVTELLNGEAaqkdasadllkilaVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNL 464
Cdd:pfam04733 181 IQDAYYIFQEfsEKYDSTPLLLNGQA--------------VCCMCLGRYEEAESLLKEALDKDAKDPETLINL 239
TPR_11 pfam13414
TPR repeat;
436-471 5.01e-03

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 34.75  E-value: 5.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1816047931 436 QIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEK 471
Cdd:pfam13414   6 EQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYKL 41
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 392-482 8.79e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 38.82  E-value: 8.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047931 392 ALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEK 471
Cdd:COG3914   148 AYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQA 227

                          90
                  ....*....|.
gi 1816047931 472 NELAQAEKAIR 482
Cdd:COG3914   228 CDWEVYDRFEE 238
 
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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