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Conserved domains on  [gi|494613984|ref|WP_007372229|]
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MULTISPECIES: DsbC family protein [Enterobacterales]

Protein Classification

DsbC family protein( domain architecture ID 10122483)

DsbC family protein such as the DsbC/DsbG homolog DsbP, which is a novel domain-swapped dimeric protein-disulfide isomerase encoded by the multidrug resistance IncA/C transferable plasmid and is associated with conjugation

CATH:  3.40.30.10
Gene Ontology:  GO:0003756
SCOP:  3000031

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
54-243 4.21e-35

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: 124.35  E-value: 4.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494613984  54 KRFVVPTNGIIALEIDGKVNLLSSNGRFVIQGTLYDTWAKKPLTTmSEITKNASIIPMKELNLNIADLRPAvwGDGPKKV 133
Cdd:cd03020    5 SVFKTPVAGLYEVVTGGGVLYTDDDGRYLIQGNLYDAKGRKDDLT-EARLAQLNAIDLSALPLDDAIVYGK--GNGKRVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494613984 134 MIFTAPGCEACAAPLSALADLDpKEFTVSVLSLGALG-PASQQRNIELYCASDRYRADRAIISGNSTQKfdQVKNCDmQA 212
Cdd:cd03020   82 YVFTDPDCPYCRKLEKELKPNA-DGVTVRIFPVPILGlPDSTAKAAAIWCAKDRAKAWTDAMSGGKVPP--PAASCD-NP 157
                        170       180       190
                 ....*....|....*....|....*....|.
gi 494613984 213 LARREVTAQILGVSMIPFIVRDDGSYVLGSP 243
Cdd:cd03020  158 VAANLALGRQLGVNGTPTIVLADGRVVPGAP 188
 
Name Accession Description Interval E-value
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
54-243 4.21e-35

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: 124.35  E-value: 4.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494613984  54 KRFVVPTNGIIALEIDGKVNLLSSNGRFVIQGTLYDTWAKKPLTTmSEITKNASIIPMKELNLNIADLRPAvwGDGPKKV 133
Cdd:cd03020    5 SVFKTPVAGLYEVVTGGGVLYTDDDGRYLIQGNLYDAKGRKDDLT-EARLAQLNAIDLSALPLDDAIVYGK--GNGKRVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494613984 134 MIFTAPGCEACAAPLSALADLDpKEFTVSVLSLGALG-PASQQRNIELYCASDRYRADRAIISGNSTQKfdQVKNCDmQA 212
Cdd:cd03020   82 YVFTDPDCPYCRKLEKELKPNA-DGVTVRIFPVPILGlPDSTAKAAAIWCAKDRAKAWTDAMSGGKVPP--PAASCD-NP 157
                        170       180       190
                 ....*....|....*....|....*....|.
gi 494613984 213 LARREVTAQILGVSMIPFIVRDDGSYVLGSP 243
Cdd:cd03020  158 VAANLALGRQLGVNGTPTIVLADGRVVPGAP 188
PRK10877 PRK10877
protein disulfide isomerase II DsbC; Provisional
59-252 1.73e-04

protein disulfide isomerase II DsbC; Provisional


Pssm-ID: 182802 [Multi-domain]  Cd Length: 232  Bit Score: 41.62  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494613984  59 PTNGIIALEIDGKVNLLSSNGRFVIQGTLYDTWAKKPLTTMSEITknasiipMKELNlniADLRPAVWGDGPKK---VMI 135
Cdd:PRK10877  44 PVAGMKTVLTESGVLYITDDGKHIIQGPMYDVSGTAPVNVTNQLL-------LKKLN---ALEKEMIVYKAPQEkhvITV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494613984 136 FTAPGCEACAAPLSALADLDPKEFTVSVLSLGALGPASQ--QRNIELYCASDRYRADRAIISGNSTQKFDqvknCDMQAL 213
Cdd:PRK10877 114 FTDITCGYCHKLHEQMKDYNALGITVRYLAFPRQGLDSQaeKDMKSIWCAADRNKAFDDAMKGKDVSPAS----CDVDIA 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 494613984 214 ARREVTAQiLGVSMIPFIVRDDGSYVLG--SPKQgLKNFIE 252
Cdd:PRK10877 190 DHYALGVQ-FGVQGTPAIVLSNGTLVPGyqGPKE-MKAFLD 228
 
Name Accession Description Interval E-value
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
54-243 4.21e-35

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: 124.35  E-value: 4.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494613984  54 KRFVVPTNGIIALEIDGKVNLLSSNGRFVIQGTLYDTWAKKPLTTmSEITKNASIIPMKELNLNIADLRPAvwGDGPKKV 133
Cdd:cd03020    5 SVFKTPVAGLYEVVTGGGVLYTDDDGRYLIQGNLYDAKGRKDDLT-EARLAQLNAIDLSALPLDDAIVYGK--GNGKRVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494613984 134 MIFTAPGCEACAAPLSALADLDpKEFTVSVLSLGALG-PASQQRNIELYCASDRYRADRAIISGNSTQKfdQVKNCDmQA 212
Cdd:cd03020   82 YVFTDPDCPYCRKLEKELKPNA-DGVTVRIFPVPILGlPDSTAKAAAIWCAKDRAKAWTDAMSGGKVPP--PAASCD-NP 157
                        170       180       190
                 ....*....|....*....|....*....|.
gi 494613984 213 LARREVTAQILGVSMIPFIVRDDGSYVLGSP 243
Cdd:cd03020  158 VAANLALGRQLGVNGTPTIVLADGRVVPGAP 188
PRK10877 PRK10877
protein disulfide isomerase II DsbC; Provisional
59-252 1.73e-04

protein disulfide isomerase II DsbC; Provisional


Pssm-ID: 182802 [Multi-domain]  Cd Length: 232  Bit Score: 41.62  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494613984  59 PTNGIIALEIDGKVNLLSSNGRFVIQGTLYDTWAKKPLTTMSEITknasiipMKELNlniADLRPAVWGDGPKK---VMI 135
Cdd:PRK10877  44 PVAGMKTVLTESGVLYITDDGKHIIQGPMYDVSGTAPVNVTNQLL-------LKKLN---ALEKEMIVYKAPQEkhvITV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494613984 136 FTAPGCEACAAPLSALADLDPKEFTVSVLSLGALGPASQ--QRNIELYCASDRYRADRAIISGNSTQKFDqvknCDMQAL 213
Cdd:PRK10877 114 FTDITCGYCHKLHEQMKDYNALGITVRYLAFPRQGLDSQaeKDMKSIWCAADRNKAFDDAMKGKDVSPAS----CDVDIA 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 494613984 214 ARREVTAQiLGVSMIPFIVRDDGSYVLG--SPKQgLKNFIE 252
Cdd:PRK10877 190 DHYALGVQ-FGVQGTPAIVLSNGTLVPGyqGPKE-MKAFLD 228
 
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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