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Conserved domains on  [gi|969849197|ref|WP_058610060|]
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MULTISPECIES: type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB [Enterobacter cloacae complex]

Protein Classification

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB( domain architecture ID 10014381)

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system

CATH:  3.40.30.10
PubMed:  16321931|15558583|10049365|12074972

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 1-184 1.46e-110

conjugal transfer protein TrbB; Provisional


:

Pssm-ID: 237484  Cd Length: 181  Bit Score: 312.81  E-value: 1.46e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197   1 MNLRHTVfTVALMTLSLATQASTMDEIKSLWHPQGARASGSLPTSPEDPevkPLPAKQPVWYRLSNGRQVNLADWKVVLF 80
Cdd:PRK13728   1 MSLTKLL-LVLLLLMATAVQASTRDEIERLWNPKGMAAQPAQPAADTSA---RTEKPAPRWFRLSNGRQVNLADWKVVLF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197  81 MQGHCPYCHQFDPVLKSLSARVGFGVMAYTIDGQGDASFPDALPAPPEVMKTFFPNLPVATPTTFLVNVNTLEALPLLQG 160
Cdd:PRK13728  77 MQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQG 156

                        170       180
                 ....*....|....*....|....
gi 969849197 161 ATDEQGFMARMDTVLQMRGVGNNG 184
Cdd:PRK13728 157 ATDAAGFMARMDTVLQMYGGKKGA 180
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 1-184 1.46e-110

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 312.81  E-value: 1.46e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197   1 MNLRHTVfTVALMTLSLATQASTMDEIKSLWHPQGARASGSLPTSPEDPevkPLPAKQPVWYRLSNGRQVNLADWKVVLF 80
Cdd:PRK13728   1 MSLTKLL-LVLLLLMATAVQASTRDEIERLWNPKGMAAQPAQPAADTSA---RTEKPAPRWFRLSNGRQVNLADWKVVLF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197  81 MQGHCPYCHQFDPVLKSLSARVGFGVMAYTIDGQGDASFPDALPAPPEVMKTFFPNLPVATPTTFLVNVNTLEALPLLQG 160
Cdd:PRK13728  77 MQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQG 156

                        170       180
                 ....*....|....*....|....
gi 969849197 161 ATDEQGFMARMDTVLQMRGVGNNG 184
Cdd:PRK13728 157 ATDAAGFMARMDTVLQMYGGKKGA 180
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 3-175 2.45e-68

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system. This protein has been predicted to contain a thioredoxin fold, contains a conserved pair of cysteines and has been shown to function as a thiol disulfide isomerase by complementation of an Ecoli DsbA defect. The protein is believed to be involved in pilin assembly. The protein is closely related to TraF (TIGR02739) which is somewhat longer, lacks the cysteine motif and is apparently not functional as a disulfide bond isomerase.


Pssm-ID: 131785  Cd Length: 153  Bit Score: 205.04  E-value: 2.45e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197    3 LRHTVFTVALMTLSLAtQASTMDEIKSLWHPqgarasgslptsPEDPEVKPLPAKQpvwyrlsnGRQVNLADWKVVLFMQ 82
Cdd:TIGR02738   1 MLRKLLIVLLLLAGLA-QASTLDEITNLWAP------------PQGLTAATDNAPQ--------GRHANQDDYALVFFYQ 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197   83 GHCPYCHQFDPVLKSLSARVGFGVMAYTIDGQGDASFPDALPAPPEVMKTFFPN-LPVATPTTFLVNVNTLEALPLLQGA 161
Cdd:TIGR02738  60 STCPYCHQFAPVLKRFSQQFGLPVYAFSLDGQGLTGFPDPLPATPEVMQTFFPNpRPVVTPATFLVNVNTRKAYPVLQGA 139

                         170
                  ....*....|....
gi 969849197  162 TDEQGFMARMDTVL 175
Cdd:TIGR02738 140 VDEAELANRMDEIL 153
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 71-161 9.02e-11

F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated with export. The 19 amino acids at the amino terminus of the polypeptides appear to constitute a typical membrane leader peptide - not included in this family, while the remainder of the molecule is predicted to be primarily hydrophilic in character. F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer, and they are both localized to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor.


Pssm-ID: 433436 [Multi-domain]  Cd Length: 224  Bit Score: 58.47  E-value: 9.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197   71 NLAD-WKVVLFMQGHCPYCHQFDPVLKSLSARVGFGVMAYTIDGQGDASFPDALPAPPEvMKTFfpNLPVaTPTTFLVNV 149
Cdd:pfam13728 126 SLAEeFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFPNYRVDNGQ-AARL--GVKR-TPALFLVNP 201

                          90
                  ....*....|..
gi 969849197  150 NTLEALPLLQGA 161
Cdd:pfam13728 202 PSGDVVPVAAGV 213
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 76-117 8.87e-04

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 38.45  E-value: 8.87e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 969849197  76 KVVLFMQGHCPYCHQFDPVLKSLSARVGFGVMAYTIDGQGDA 117
Cdd:cd03020   80 VVYVFTDPDCPYCRKLEKELKPNADGVTVRIFPVPILGLPDS 121
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 66-148 1.09e-03

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 37.75  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197  66 NGRQVNLADW--KVVL--FMQGHCPYCHQFDPVLKSLSARV-GFGVMAYTIDGQGDA----------SFPDALPAPPEVM 130
Cdd:COG0526   17 DGKPLSLADLkgKPVLvnFWATWCPPCRAEMPVLKELAEEYgGVVFVGVDVDENPEAvkaflkelglPYPVLLDPDGELA 96

                         90
                 ....*....|....*....
gi 969849197 131 KTFfpnlPV-ATPTTFLVN 148
Cdd:COG0526   97 KAY----GVrGIPTTVLID 111
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 1-184 1.46e-110

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 312.81  E-value: 1.46e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197   1 MNLRHTVfTVALMTLSLATQASTMDEIKSLWHPQGARASGSLPTSPEDPevkPLPAKQPVWYRLSNGRQVNLADWKVVLF 80
Cdd:PRK13728   1 MSLTKLL-LVLLLLMATAVQASTRDEIERLWNPKGMAAQPAQPAADTSA---RTEKPAPRWFRLSNGRQVNLADWKVVLF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197  81 MQGHCPYCHQFDPVLKSLSARVGFGVMAYTIDGQGDASFPDALPAPPEVMKTFFPNLPVATPTTFLVNVNTLEALPLLQG 160
Cdd:PRK13728  77 MQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQG 156

                        170       180
                 ....*....|....*....|....
gi 969849197 161 ATDEQGFMARMDTVLQMRGVGNNG 184
Cdd:PRK13728 157 ATDAAGFMARMDTVLQMYGGKKGA 180
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 3-175 2.45e-68

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system. This protein has been predicted to contain a thioredoxin fold, contains a conserved pair of cysteines and has been shown to function as a thiol disulfide isomerase by complementation of an Ecoli DsbA defect. The protein is believed to be involved in pilin assembly. The protein is closely related to TraF (TIGR02739) which is somewhat longer, lacks the cysteine motif and is apparently not functional as a disulfide bond isomerase.


Pssm-ID: 131785  Cd Length: 153  Bit Score: 205.04  E-value: 2.45e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197    3 LRHTVFTVALMTLSLAtQASTMDEIKSLWHPqgarasgslptsPEDPEVKPLPAKQpvwyrlsnGRQVNLADWKVVLFMQ 82
Cdd:TIGR02738   1 MLRKLLIVLLLLAGLA-QASTLDEITNLWAP------------PQGLTAATDNAPQ--------GRHANQDDYALVFFYQ 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197   83 GHCPYCHQFDPVLKSLSARVGFGVMAYTIDGQGDASFPDALPAPPEVMKTFFPN-LPVATPTTFLVNVNTLEALPLLQGA 161
Cdd:TIGR02738  60 STCPYCHQFAPVLKRFSQQFGLPVYAFSLDGQGLTGFPDPLPATPEVMQTFFPNpRPVVTPATFLVNVNTRKAYPVLQGA 139

                         170
                  ....*....|....
gi 969849197  162 TDEQGFMARMDTVL 175
Cdd:TIGR02738 140 VDEAELANRMDEIL 153
TraF-like TIGR02740
TraF-like protein; This protein is related to the F-type conjugation system pilus assembly ...
 80-170 2.26e-11

TraF-like protein; This protein is related to the F-type conjugation system pilus assembly proteins TraF (TIGR02739)and TrbB (TIGR02738) both of which exhibit a thioredoxin fold. The protein represented by this model has the same length and architecture as TraF, but lacks the CXXC-motif found in TrbB and believed to be responsible for the disulfide isomerase activity of that protein.


Pssm-ID: 274275  Cd Length: 271  Bit Score: 60.89  E-value: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197   80 FMQGHCPYCHQFDPVLKSLSARVGFGVMAYTIDGQGDASFPDALPAPPEVMKtffpnLPVAT-PTTFLVNVNTLEALPLL 158
Cdd:TIGR02740 173 FFKSDCPYCHQQAPILQAFEDRYGIEVLPVSVDGGPLPGFPNARPDAGQAQQ-----LKIRTvPAVFLADPDPNQFTPIG 247

                          90
                  ....*....|..
gi 969849197  159 QGATDEQGFMAR 170
Cdd:TIGR02740 248 FGVMSADELVDR 259
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 71-161 9.02e-11

F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated with export. The 19 amino acids at the amino terminus of the polypeptides appear to constitute a typical membrane leader peptide - not included in this family, while the remainder of the molecule is predicted to be primarily hydrophilic in character. F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer, and they are both localized to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor.


Pssm-ID: 433436 [Multi-domain]  Cd Length: 224  Bit Score: 58.47  E-value: 9.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197   71 NLAD-WKVVLFMQGHCPYCHQFDPVLKSLSARVGFGVMAYTIDGQGDASFPDALPAPPEvMKTFfpNLPVaTPTTFLVNV 149
Cdd:pfam13728 126 SLAEeFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFPNYRVDNGQ-AARL--GVKR-TPALFLVNP 201

                          90
                  ....*....|..
gi 969849197  150 NTLEALPLLQGA 161
Cdd:pfam13728 202 PSGDVVPVAAGV 213
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 76-117 8.87e-04

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 38.45  E-value: 8.87e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 969849197  76 KVVLFMQGHCPYCHQFDPVLKSLSARVGFGVMAYTIDGQGDA 117
Cdd:cd03020   80 VVYVFTDPDCPYCRKLEKELKPNADGVTVRIFPVPILGLPDS 121
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 66-148 1.09e-03

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 37.75  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197  66 NGRQVNLADW--KVVL--FMQGHCPYCHQFDPVLKSLSARV-GFGVMAYTIDGQGDA----------SFPDALPAPPEVM 130
Cdd:COG0526   17 DGKPLSLADLkgKPVLvnFWATWCPPCRAEMPVLKELAEEYgGVVFVGVDVDENPEAvkaflkelglPYPVLLDPDGELA 96

                         90
                 ....*....|....*....
gi 969849197 131 KTFfpnlPV-ATPTTFLVN 148
Cdd:COG0526   97 KAY----GVrGIPTTVLID 111
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
75-148 3.41e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 35.48  E-value: 3.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 969849197   75 WKVVLFMQGHCPYCHQFDPVLKSLSA---RVGFGVMAYTIDGQGDASFPDALPAPPEVMKtFFPNLPV-ATPTTFLVN 148
Cdd:pfam13098   6 PVLVVFTDPDCPYCKKLKKELLEDPDvtvYLGPNFVFIAVNIWCAKEVAKAFTDILENKE-LGRKYGVrGTPTIVFFD 82
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
66-148 4.38e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 35.61  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969849197  66 NGRQVNLADWK----VVLFMQGHCPYC----HQFDPVLKSLSARvGFGVMAYTIDgqgdasfpdalpaPPEVMKTF---- 133
Cdd:COG1225   10 DGKTVSLSDLRgkpvVLYFYATWCPGCtaelPELRDLYEEFKDK-GVEVLGVSSD-------------SDEAHKKFaeky 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 969849197 134 ---FPNLP------------VATPTTFLVN 148
Cdd:COG1225   76 glpFPLLSdpdgevakaygvRGTPTTFLID 105
 
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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