Thiol:disulfide interchange protein DsbC
Details
- Name
- Thiol:disulfide interchange protein DsbC
- Synonyms
- xprA
- Gene Name
- dsbC
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011503|Thiol:disulfide interchange protein DsbC MKKGFMLFTLLAAFSGFAQADDAAIQQTLAKMGIKSSDIQPAPVAGMKTVLTNSGVLYIT DDGKHIIQGPMYDVSGTAPVNVTNKMLLKQLNALEKEMIVYKAPQEKHVITVFTDITCGY CHKLHEQMADYNALGITVRYLAFPRQGLDSDAEKEMKAIWCAKDKNKAFDDVMAGKSVAP ASCDVDIADHYALGVQLGVSGTPAVVLSNGTLVPGYQPPKEMKEFLDEHQKMTSGK
- Number of residues
- 236
- Molecular Weight
- 25621.495
- Theoretical pI
- 6.78
- GO Classification
- Functionsprotein disulfide isomerase activity / protein disulfide oxidoreductase activityProcessescell redox homeostasis / oxidation-reduction process / protein foldingComponentsouter membrane-bounded periplasmic space / periplasmic space
- General Function
- Protein disulfide oxidoreductase activity
- Specific Function
- Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0011504|Thiol:disulfide interchange protein DsbC (dsbC) ATGAAGAAAGGTTTTATGTTGTTTACTTTGTTAGCGGCGTTTTCAGGCTTTGCTCAGGCT GATGACGCGGCAATTCAACAAACGTTAGCCAAAATGGGCATCAAAAGCAGCGATATTCAG CCCGCGCCTGTAGCTGGCATGAAGACAGTTCTGACTAACAGCGGCGTGTTGTACATCACC GATGATGGTAAACATATCATTCAGGGGCCAATGTATGACGTTAGTGGCACGGCTCCGGTC AATGTCACCAATAAGATGCTGTTAAAGCAGTTGAATGCGCTTGAAAAAGAGATGATCGTT TATAAAGCGCCGCAGGAAAAACACGTCATCACCGTGTTTACTGATATTACCTGTGGTTAC TGCCACAAACTGCATGAGCAAATGGCAGACTACAACGCGCTGGGGATCACCGTGCGTTAT CTTGCTTTCCCGCGCCAGGGGCTGGACAGCGATGCAGAGAAAGAAATGAAAGCTATCTGG TGTGCGAAAGATAAAAACAAAGCGTTTGATGATGTGATGGCAGGTAAAAGCGTCGCACCA GCCAGTTGCGACGTGGATATTGCCGACCATTACGCACTTGGCGTCCAGCTTGGCGTTAGC GGTACTCCGGCAGTTGTGCTGAGCAATGGCACACTTGTTCCGGGTTACCAGCCGCCGAAA GAGATGAAAGAATTCCTCGACGAACACCAAAAAATGACCAGCGGTAAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0AEG6 UniProtKB Entry Name DSBC_ECOLI GenBank Gene ID M54884 - General References
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- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
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- Missiakas D, Georgopoulos C, Raina S: The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 1994 Apr 15;13(8):2013-20. [Article]
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- Shevchik VE, Condemine G, Robert-Baudouy J: Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J. 1994 Apr 15;13(8):2007-12. [Article]
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- Depuydt M, Leonard SE, Vertommen D, Denoncin K, Morsomme P, Wahni K, Messens J, Carroll KS, Collet JF: A periplasmic reducing system protects single cysteine residues from oxidation. Science. 2009 Nov 20;326(5956):1109-11. doi: 10.1126/science.1179557. [Article]
- McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P: Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nat Struct Biol. 2000 Mar;7(3):196-9. [Article]