EC Number | Cloned (Comment) | Organism |
---|---|---|
1.8.4.15 | gene dsbA, recombinant expression of recombinant enzyme in Escherichia coli, coexpression with Chlamydia trachomatis dsbB | Chlamydia trachomatis |
1.8.5.9 | expressed in Escherichia coli C41(DE3) cells | Chlamydia trachomatis |
1.8.5.9 | gene dsbB, recombinant expression of recombinant enzyme in Escherichia coli, coexpression with Chlamydia trachomatis dsbA | Chlamydia trachomatis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.8.5.9 | additional information | construction of mutant CtDsbB-CCSS, in which periplasmic loop 2 Cys98 and Cys104 are mutated to serines. In the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA | Chlamydia trachomatis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.8.4.15 | inclusion vacuole | CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds | Chlamydia trachomatis | - |
- |
1.8.4.15 | periplasm | - |
Chlamydia trachomatis | - |
- |
1.8.5.9 | membrane | - |
Chlamydia trachomatis | 16020 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.5.9 | [DsbA protein] with reduced L-cysteine residues + quinone | Chlamydia trachomatis | overall reaction | [DsbA protein] carrying a disulfide bond + quinol | - |
? | |
1.8.5.9 | [DsbA protein] with reduced L-cysteine residues + quinone | Chlamydia trachomatis A2497 | overall reaction | [DsbA protein] carrying a disulfide bond + quinol | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.4.15 | Chlamydia trachomatis | G4NNC6 | - |
- |
1.8.4.15 | Chlamydia trachomatis A2497 | G4NNC6 | - |
- |
1.8.5.9 | Chlamydia trachomatis | - |
- |
- |
1.8.5.9 | Chlamydia trachomatis | G4NNC5 | serovar A | - |
1.8.5.9 | Chlamydia trachomatis A2497 | G4NNC5 | serovar A | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.8.5.9 | His-Trap column chromatography and Superdex 200 gel filtration | Chlamydia trachomatis |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.8.4.15 | additional information | enzyme CtDsbA is expressed early in the Chlamydial trachomatis developmental cycle | Chlamydia trachomatis | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.4.15 | additional information | membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA | Chlamydia trachomatis | ? | - |
- |
|
1.8.4.15 | additional information | membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA | Chlamydia trachomatis A2497 | ? | - |
- |
|
1.8.5.9 | additional information | membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA, the active site CSAC thiols are the likely target for CtDsbB mediated oxidation | Chlamydia trachomatis | ? | - |
- |
|
1.8.5.9 | additional information | membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA, the active site CSAC thiols are the likely target for CtDsbB mediated oxidation | Chlamydia trachomatis A2497 | ? | - |
- |
|
1.8.5.9 | [DsbA protein] with reduced L-cysteine residues + quinone | overall reaction | Chlamydia trachomatis | [DsbA protein] carrying a disulfide bond + quinol | - |
? | |
1.8.5.9 | [DsbA protein] with reduced L-cysteine residues + quinone | overall reaction | Chlamydia trachomatis A2497 | [DsbA protein] carrying a disulfide bond + quinol | - |
? | |
1.8.5.9 | [DsbA protein] with reduced L-cysteine residues + ubiquinone-1 | overall reaction | Chlamydia trachomatis | [DsbA protein] carrying a disulfide bond + ubiquinol-1 | - |
? | |
1.8.5.9 | [DsbA protein] with reduced L-cysteine residues + ubiquinone-1 | overall reaction | Chlamydia trachomatis A2497 | [DsbA protein] carrying a disulfide bond + ubiquinol-1 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.8.4.15 | C. trachomatis disulfide bond protein A | - |
Chlamydia trachomatis |
1.8.4.15 | CtDsbA | - |
Chlamydia trachomatis |
1.8.4.15 | DsbA | - |
Chlamydia trachomatis |
1.8.5.9 | C. trachomatis disulfide bond protein B | - |
Chlamydia trachomatis |
1.8.5.9 | CtDsbB | - |
Chlamydia trachomatis |
1.8.5.9 | disulfide bond protein B | - |
Chlamydia trachomatis |
1.8.5.9 | DsbB | - |
Chlamydia trachomatis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.8.4.15 | additional information | - |
the melting temperatures (Tm) of reduced and oxidised CtDsbA are similar | Chlamydia trachomatis |
EC Number | Organism | Comment | Expression |
---|---|---|---|
1.8.4.15 | Chlamydia trachomatis | CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds | up |
1.8.5.9 | Chlamydia trachomatis | CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds | up |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.8.4.15 | evolution | while CtDsbA shares common structural and biochemical features with the DsbA-II group of DsbA proteins, especially, CtDsbA shares just 15% sequence identity with the canonical EcDsbA protein and approximately 20% sequence identity with other members of the structurally characterised DsbA-II class proteins that contain a second disulfide. The second disulfide of CtDsbA does not influence interaction with CtDsbB | Chlamydia trachomatis |
1.8.4.15 | additional information | the classic DsbA structure consists of a thioredoxin domain and an inserted alpha-helical bundle domain. The enzyme's active site is a Cys-Xaa-Xaa-Cys motif located at the N-terminus of helix H1. The sequence of the Xaa-Xaa dipeptide modulates the redox character of the enzyme. The catalytic surface of the protein features 3 loops: loop 1, (linking helix H1 and beta-strand B3), loop 2 (linking helix H6 and beta-strand B4) which contains a highly conserved cis-Pro residue, and loop 3 (linking helix H7 and beta-strand B5.) Together these loops govern the enzyme's redox properties and its interactions with protein substrates. CtDsbA has a second, non-catalytic disulfide, in addition to the enzymatically critical active site disulfide, this non-catalytic disulfide staples H3 and H5 of the inserted alpha-helix domain. In mutant CtDsbB-CCSS periplasmic loop 2 Cys98 and Cys104 are mutated to serines, in the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA. The second disulfide of CtDsbA does not influence interaction with CtDsbB | Chlamydia trachomatis |
1.8.4.15 | physiological function | disulfide bond protein A (DsbA) is the primary oxidase in the disulfide oxidative pathway of bacteria. DsbA catalyses the introduction of disulfide bonds into reduced and folding proteins in concert with a membrane protein partner DsbB. DsbB uses a quinone cofactor as an electron acceptor, and together the DsbA-DsbB pair ultimately shuttle electrons from a reduced protein substrate to molecular oxygen via the respiratory pathway. CtDsbA is directly oxidised by CtDsbB, in a reaction in which both periplasmic cysteine pairs of CtDsbB are required for complete activity. Potential role of CtDsbA in chlamydial envelope disulfide bonding, and importance of disulfide crosslinking of the Chlamydia envelope in infection and Chlamydia development | Chlamydia trachomatis |
1.8.5.9 | physiological function | disulfide bond protein A (DsbA) is the primary oxidase in the disulfide oxidative pathway of bacteria. DsbA catalyses the introduction of disulfide bonds into reduced and folding proteins in concert with a membrane protein partner DsbB. DsbB uses a quinone cofactor as an electron acceptor, and together the DsbA-DsbB pair ultimately shuttle electrons from a reduced protein substrate to molecular oxygen via the respiratory pathway. CtDsbA is directly oxidised by CtDsbB, in a reaction in which both periplasmic cysteine pairs of CtDsbB are required for complete activity. The second disulfide of CtDsbA does not influence interaction with CtDsbB | Chlamydia trachomatis |