IncI1-type conjugal transfer protein TrbB (plasmid) [Escherichia coli]
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
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 ... |
129-346 | 1.59e-42 | ||||
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: 146.69 E-value: 1.59e-42
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| Name | Accession | Description | Interval | E-value | ||||
| DsbA_DsbC_DsbG | cd03020 | DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ... |
129-346 | 1.59e-42 | ||||
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: 146.69 E-value: 1.59e-42
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| DsbG | COG1651 | Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ... |
211-321 | 5.55e-06 | ||||
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441257 [Multi-domain] Cd Length: 152 Bit Score: 45.76 E-value: 5.55e-06
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| TraF | pfam13728 | F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ... |
170-250 | 2.45e-03 | ||||
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: 38.83 E-value: 2.45e-03
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| Name | Accession | Description | Interval | E-value | ||||
| DsbA_DsbC_DsbG | cd03020 | DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ... |
129-346 | 1.59e-42 | ||||
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: 146.69 E-value: 1.59e-42
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| DsbG | COG1651 | Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ... |
211-321 | 5.55e-06 | ||||
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441257 [Multi-domain] Cd Length: 152 Bit Score: 45.76 E-value: 5.55e-06
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| DsbA_Com1_like | cd03023 | DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ... |
212-327 | 3.29e-05 | ||||
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: 43.35 E-value: 3.29e-05
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| DsbA_family | cd02972 | DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ... |
216-276 | 1.31e-04 | ||||
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: 40.47 E-value: 1.31e-04
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| TraF | pfam13728 | F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ... |
170-250 | 2.45e-03 | ||||
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: 38.83 E-value: 2.45e-03
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| Blast search parameters | ||||
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