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Conserved domains on  [gi|2527343828|ref|WP_288366331|]
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DsbC family protein [uncultured Marinobacter sp.]

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
PubMed:  11967064|10391895|10788443|9099998|10049365|15558583
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 ...
 42-238 3.25e-62

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: 193.30  E-value: 3.25e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828  42 LKVVSVKESEAKGLYEVQSNNGdTIYATEDGQYLMTGDLLKITDqGIANVTEAARTEARREMMADYGNKGVISFPAKNEK 121
Cdd:cd03020     1 TKVDSVFKTPVAGLYEVVTGGG-VLYTDDDGRYLIQGNLYDAKG-RKDDLTEARLAQLNAIDLSALPLDDAIVYGKGNGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 122 AVVNVFTDIDCPYCRKLHDEVPQLNGyGITVNYYAFPRSGpNTASFKKYESVWCADDQQAAMDAAKAGRSV--PDASCEN 199
Cdd:cd03020    79 RVVYVFTDPDCPYCRKLEKELKPNAD-GVTVRIFPVPILG-LPDSTAKAAAIWCAKDRAKAWTDAMSGGKVppPAASCDN 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2527343828 200 PVGEQYELGGRAGVTGTPAIVLEDGSMIRGYVPAQRLAE 238
Cdd:cd03020   157 PVAANLALGRQLGVNGTPTIVLADGRVVPGAPPAAQLEA 195
 
Name Accession Description Interval E-value
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 42-238 3.25e-62

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: 193.30  E-value: 3.25e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828  42 LKVVSVKESEAKGLYEVQSNNGdTIYATEDGQYLMTGDLLKITDqGIANVTEAARTEARREMMADYGNKGVISFPAKNEK 121
Cdd:cd03020     1 TKVDSVFKTPVAGLYEVVTGGG-VLYTDDDGRYLIQGNLYDAKG-RKDDLTEARLAQLNAIDLSALPLDDAIVYGKGNGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 122 AVVNVFTDIDCPYCRKLHDEVPQLNGyGITVNYYAFPRSGpNTASFKKYESVWCADDQQAAMDAAKAGRSV--PDASCEN 199
Cdd:cd03020    79 RVVYVFTDPDCPYCRKLEKELKPNAD-GVTVRIFPVPILG-LPDSTAKAAAIWCAKDRAKAWTDAMSGGKVppPAASCDN 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2527343828 200 PVGEQYELGGRAGVTGTPAIVLEDGSMIRGYVPAQRLAE 238
Cdd:cd03020   157 PVAANLALGRQLGVNGTPTIVLADGRVVPGAPPAAQLEA 195
PRK10877 PRK10877
protein disulfide isomerase II DsbC; Provisional
 41-240 1.44e-57

protein disulfide isomerase II DsbC; Provisional


Pssm-ID: 182802 [Multi-domain]  Cd Length: 232  Bit Score: 182.60  E-value: 1.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828  41 GLKVVSVKESEAKGLYEVQSNNGdTIYATEDGQYLMTGDLLKITDQGIANVTEAA---RTEARREMMadygnkgvISFPA 117
Cdd:PRK10877   34 GIQSADIQPSPVAGMKTVLTESG-VLYITDDGKHIIQGPMYDVSGTAPVNVTNQLllkKLNALEKEM--------IVYKA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 118 KNEKAVVNVFTDIDCPYCRKLHDEVPQLNGYGITVNYYAFPRSGPNTASFKKYESVWCADDQQAAMDAAKAGRSVPDASC 197
Cdd:PRK10877  105 PQEKHVITVFTDITCGYCHKLHEQMKDYNALGITVRYLAFPRQGLDSQAEKDMKSIWCAADRNKAFDDAMKGKDVSPASC 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2527343828 198 ENPVGEQYELGGRAGVTGTPAIVLEDGSMIRGYVPAQRLAEGL 240
Cdd:PRK10877  185 DVDIADHYALGVQFGVQGTPAIVLSNGTLVPGYQGPKEMKAFL 227
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
117-238 2.86e-23

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 90.18  E-value: 2.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 117 AKNEKAVVNVFTDIDCPYCRKLHDEVPQLNGYGITVnyyafprsgpNTASFKKYESVWCADDQQAAMDAakagrsvpdas 196
Cdd:pfam13098   1 KGNGKPVLVVFTDPDCPYCKKLKKELLEDPDVTVYL----------GPNFVFIAVNIWCAKEVAKAFTD----------- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2527343828 197 cenpVGEQYELGGRAGVTGTPAIVLEDGS----MIRGYVPAQRLAE 238
Cdd:pfam13098  60 ----ILENKELGRKYGVRGTPTIVFFDGKgellRLPGYVPAEEFLA 101
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 121-238 7.52e-22

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 88.13  E-value: 7.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 121 KAVVNVFTDIDCPYCRKLHDEVPQLN---GYG-ITVNYYAFPRSGPNtaSFKKYESVWCADDQ----------------- 179
Cdd:COG1651     1 KVTVVEFFDYQCPYCARFHPELPELLkkyVDGkVRVVYRPFPLLHPD--SLRAARAALCAADQgkfwafhdalfanqpal 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527343828 180 ----------QAAMDAAKAGRSVPDASCENPVGEQYELGGRAGVTGTPAIVLeDGSMIRGYVPAQRLAE 238
Cdd:COG1651    79 tdddlreiakEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVV-NGKLVSGAVPYEELEA 146
 
Name Accession Description Interval E-value
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 42-238 3.25e-62

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: 193.30  E-value: 3.25e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828  42 LKVVSVKESEAKGLYEVQSNNGdTIYATEDGQYLMTGDLLKITDqGIANVTEAARTEARREMMADYGNKGVISFPAKNEK 121
Cdd:cd03020     1 TKVDSVFKTPVAGLYEVVTGGG-VLYTDDDGRYLIQGNLYDAKG-RKDDLTEARLAQLNAIDLSALPLDDAIVYGKGNGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 122 AVVNVFTDIDCPYCRKLHDEVPQLNGyGITVNYYAFPRSGpNTASFKKYESVWCADDQQAAMDAAKAGRSV--PDASCEN 199
Cdd:cd03020    79 RVVYVFTDPDCPYCRKLEKELKPNAD-GVTVRIFPVPILG-LPDSTAKAAAIWCAKDRAKAWTDAMSGGKVppPAASCDN 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2527343828 200 PVGEQYELGGRAGVTGTPAIVLEDGSMIRGYVPAQRLAE 238
Cdd:cd03020   157 PVAANLALGRQLGVNGTPTIVLADGRVVPGAPPAAQLEA 195
PRK10877 PRK10877
protein disulfide isomerase II DsbC; Provisional
 41-240 1.44e-57

protein disulfide isomerase II DsbC; Provisional


Pssm-ID: 182802 [Multi-domain]  Cd Length: 232  Bit Score: 182.60  E-value: 1.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828  41 GLKVVSVKESEAKGLYEVQSNNGdTIYATEDGQYLMTGDLLKITDQGIANVTEAA---RTEARREMMadygnkgvISFPA 117
Cdd:PRK10877   34 GIQSADIQPSPVAGMKTVLTESG-VLYITDDGKHIIQGPMYDVSGTAPVNVTNQLllkKLNALEKEM--------IVYKA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 118 KNEKAVVNVFTDIDCPYCRKLHDEVPQLNGYGITVNYYAFPRSGPNTASFKKYESVWCADDQQAAMDAAKAGRSVPDASC 197
Cdd:PRK10877  105 PQEKHVITVFTDITCGYCHKLHEQMKDYNALGITVRYLAFPRQGLDSQAEKDMKSIWCAADRNKAFDDAMKGKDVSPASC 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2527343828 198 ENPVGEQYELGGRAGVTGTPAIVLEDGSMIRGYVPAQRLAEGL 240
Cdd:PRK10877  185 DVDIADHYALGVQFGVQGTPAIVLSNGTLVPGYQGPKEMKAFL 227
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
117-238 2.86e-23

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 90.18  E-value: 2.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 117 AKNEKAVVNVFTDIDCPYCRKLHDEVPQLNGYGITVnyyafprsgpNTASFKKYESVWCADDQQAAMDAakagrsvpdas 196
Cdd:pfam13098   1 KGNGKPVLVVFTDPDCPYCKKLKKELLEDPDVTVYL----------GPNFVFIAVNIWCAKEVAKAFTD----------- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2527343828 197 cenpVGEQYELGGRAGVTGTPAIVLEDGS----MIRGYVPAQRLAE 238
Cdd:pfam13098  60 ----ILENKELGRKYGVRGTPTIVFFDGKgellRLPGYVPAEEFLA 101
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 121-238 7.52e-22

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 88.13  E-value: 7.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 121 KAVVNVFTDIDCPYCRKLHDEVPQLN---GYG-ITVNYYAFPRSGPNtaSFKKYESVWCADDQ----------------- 179
Cdd:COG1651     1 KVTVVEFFDYQCPYCARFHPELPELLkkyVDGkVRVVYRPFPLLHPD--SLRAARAALCAADQgkfwafhdalfanqpal 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527343828 180 ----------QAAMDAAKAGRSVPDASCENPVGEQYELGGRAGVTGTPAIVLeDGSMIRGYVPAQRLAE 238
Cdd:COG1651    79 tdddlreiakEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVV-NGKLVSGAVPYEELEA 146
DsbC_N pfam10411
Disulfide bond isomerase protein N-terminus; This is the N-terminal domain of the disulfide ...
 33-86 1.55e-13

Disulfide bond isomerase protein N-terminus; This is the N-terminal domain of the disulfide bond isomerase DsbC. The whole molecule is V-shaped, where each arm is a DsbC monomer of two domains linked by a hinge; and the N-termini of each monomer join to form the dimer interface at the base of the V, so are vital for dimerization. DsbC is required for disulfide bond formation and functions as a disulfide bond isomerase during oxidative protein-folding in bacterial periplasm. It also has chaperone activity.


Pssm-ID: 431267 [Multi-domain]  Cd Length: 54  Bit Score: 63.26  E-value: 1.55e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2527343828  33 ERLTQAVPGLKVVSVKESEAKGLYEVQSnNGDTIYATEDGQYLMTGDLLKITDQ 86
Cdd:pfam10411   2 AALEKRFPNLKVDSVSPSPVPGLYEVVT-GGQVLYTDEDGRYLIQGRLYDLKTR 54
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 126-224 7.61e-13

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270 [Multi-domain]  Cd Length: 98  Bit Score: 62.81  E-value: 7.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 126 VFTDIDCPYCRKLHDEVPQL---NGYGITVNYYAFPRSGP-NTASFKKYESVWCADDQQAAMDAAKAgrsvpdascenpv 201
Cdd:cd02972     3 EFFDPLCPYCYLFEPELEKLlyaDDGGVRVVYRPFPLLGGmPPNSLAAARAALAAAAQGKFEALHEA------------- 69

                          90       100
                  ....*....|....*....|...
gi 2527343828 202 GEQYELGGRAGVTGTPAIVLEDG 224
Cdd:cd02972    70 LADTALARALGVTGTPTFVVNGE 92
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 117-238 4.29e-07

DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.


Pssm-ID: 239321 [Multi-domain]  Cd Length: 154  Bit Score: 48.36  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 117 AKNEKAVVNVFTDIDCPYCRKLHDEVPQL---NGyGITVNYYAFPRSGPNTASFKKY-ESVWCAD--------------- 177
Cdd:cd03023     2 NPNGDVTIVEFFDYNCGYCKKLAPELEKLlkeDP-DVRVVFKEFPILGESSVLAARVaLAVWKNGpgkylefhnalmatr 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527343828 178 ---DQQAAMDAAKAG--------RSVPDASCENPVGEQYELGGRAGVTGTPAIVLEDgSMIRGYVPAQRLAE 238
Cdd:cd03023    81 grlNEESLLRIAKKAgldeaklkKDMDDPEIEATIDKNRQLARALGITGTPAFIIGD-TVIPGAVPADTLKE 151
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 117-236 1.09e-05

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 44.12  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828 117 AKNEKAVVNVFTDIDCPYCRKLHDEV---PQLNGYgITVNYYA----FPRSGPNTasfkkyesvwcaddqqaamdaakag 189
Cdd:COG2143    37 KAEGKPILLFFESDWCPYCKKLHKEVfsdPEVAAY-LKENFVVvqldAEGDKEVT------------------------- 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2527343828 190 rsvpdasceNPVGEQY---ELGGRAGVTGTPAIVL--EDGSMI---RGYVPAQRL 236
Cdd:COG2143    91 ---------DFDGETLtekELARKYGVRGTPTLVFfdAEGKEIariPGYLKPETF 136
dsbG PRK11657
disulfide isomerase/thiol-disulfide oxidase; Provisional
 61-138 1.38e-05

disulfide isomerase/thiol-disulfide oxidase; Provisional


Pssm-ID: 183262 [Multi-domain]  Cd Length: 251  Bit Score: 44.96  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343828  61 NNGDTIYATEDGQYLMTGDLLkitDQGIANVTEAARTEA-----RREMMADYGNKGVISFPAKNEKAVVNVFTDIDCPYC 135
Cdd:PRK11657   56 DMGVTIYLTPDGKHAISGYMY---DEKGENLSEALLEKEvyapmGREMWQRLEQSHWILDGKADAPRIVYVFADPNCPYC 132


                  ...
gi 2527343828 136 RKL 138
Cdd:PRK11657  133 KQF 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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