Thiol:disulfide interchange protein DsbC (P0AEG6)

Identification
Name:Thiol:disulfide interchange protein DsbC
Synonyms:Not Available
Gene Name:dsbC
Enzyme Class:
Biological Properties
General Function:Involved in cell redox homeostasis
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
Cellular Location:Periplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Complex Reactions:
1.0fused thiol:disulfide interchange protein (reduced)+1.0protein disulfide isomerase II (oxidized) → 1.0fused thiol:disulfide interchange protein (oxidized)+1.0protein disulfide isomerase II (reduced)
1.0fused thiol:disulfide interchange protein (reduced) + 1.0protein disulfide isomerase II (oxidized) → 1.0fused thiol:disulfide interchange protein (oxidized) + 1.0protein disulfide isomerase II (reduced)
ReactionCard
1.0protein disulfide isomerase II (oxidized)+2.0Thumb → 1.0protein disulfide isomerase II (reduced)+1.0Thumb
1.0protein disulfide isomerase II (oxidized) + 2.0Glutathione → 1.0protein disulfide isomerase II (reduced) + 1.0Glutathione disulfide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00125GlutathioneMetaboCard
ECMDB21221Glutathione disulfideMetaboCard
GO Classification:
Process
cell redox homeostasis
cellular homeostasis
cellular process
Gene Properties
Blattner:b2893
Gene OrientationCounterclockwise
Centisome Percentage:65.44
Left Sequence End3036134
Right Sequence End3036844
Gene Sequence:
>711 bp
ATGGTGAAAAAAGCGATAGTGACAGCGATGGCTGTAATCAGCCTCTTTACTCTGATGGGA
TGTAATAATCGGGCCGAAGTCGATACGCTTTCTCCGGCGCAGGCTGCCGAACTGAAACCG
ATGCCGCAAAGTTGGCGCGGCGTGCTGCCGTGTGCCGATTGCGAAGGAATCGAAACCTCT
CTGTTCCTCGAAAAAGACGGAACATGGGTGATGAATGAGCGTTATCTCGGTGCTCGTGAA
GAACCTTCCTCCTTCGCTTCCTACGGTACATGGGCGCGAACCGCTGACAAGCTGGTATTA
ACCGACAGCAAAGGTGAAAAGTCATATTATCGGGCGAAAGGCGATGCGCTGGAGATGCTC
GATCGTGAAGGCAATCCGATTGAATCGCAGTTCAACTATACGCTGGAAGCGGCACAATCC
AGTTTACCTATGACGCCGATGACCCTGCGGGGCATGTATTTTTATATGGCTGATGCGGCG
ACCTTCACTGATTGCGCGACCGGAAAACGTTTCATGGTAGCGAATAACGCAGAGCTGGAG
CGTAGCTACCTGGCTGCGCGCGGTCACAGTGAAAAACCGGTGTTACTGTCAGTAGAAGGT
CACTTTACGCTTGAGGGTAATCCGGATACCGGTGCGCCGACTAAAGTATTGGCACCCGAT
ACGGCAGGGAAATTTTACCCCAACCAGGATTGCAGTAGTTTGGGGCAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:236
Protein Molecular Weight:25622
Protein Theoretical pI:7
PDB File:1EEJ
Signaling Regions:
  • 1-20
Transmembrane Regions:
  • None
Protein Sequence:
>Thiol:disulfide interchange protein DsbC
MKKGFMLFTLLAAFSGFAQADDAAIQQTLAKMGIKSSDIQPAPVAGMKTVLTNSGVLYIT
DDGKHIIQGPMYDVSGTAPVNVTNKMLLKQLNALEKEMIVYKAPQEKHVITVFTDITCGY
CHKLHEQMADYNALGITVRYLAFPRQGLDSDAEKEMKAIWCAKDKNKAFDDVMAGKSVAP
ASCDVDIADHYALGVQLGVSGTPAVVLSNGTLVPGYQPPKEMKEFLDEHQKMTSGK
References
External Links:
ResourceLink
Uniprot ID:P0AEG6
Uniprot Name:DSBC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902934
PDB ID:1EEJ
Ecogene ID:EG11070
Ecocyc:EG11070
ColiBase:b2893
Kegg Gene:b2893
EchoBASE ID:EB1063
CCDB:DSBC_ECOLI
BacMap:16130795
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Depuydt, M., Leonard, S. E., Vertommen, D., Denoncin, K., Morsomme, P., Wahni, K., Messens, J., Carroll, K. S., Collet, J. F. (2009). "A periplasmic reducing system protects single cysteine residues from oxidation." Science 326:1109-1111. Pubmed: 19965429
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Joly, J. C., Swartz, J. R. (1997). "In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC." Biochemistry 36:10067-10072. Pubmed: 9254601
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Lovett, S. T., Kolodner, R. D. (1991). "Nucleotide sequence of the Escherichia coli recJ chromosomal region and construction of recJ-overexpression plasmids." J Bacteriol 173:353-364. Pubmed: 1987126
  • McCarthy, A. A., Haebel, P. W., Torronen, A., Rybin, V., Baker, E. N., Metcalf, P. (2000). "Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli." Nat Struct Biol 7:196-199. Pubmed: 10700276
  • Missiakas, D., Georgopoulos, C., Raina, S. (1994). "The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation." EMBO J 13:2013-2020. Pubmed: 8168498
  • Shevchik, V. E., Condemine, G., Robert-Baudouy, J. (1994). "Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity." EMBO J 13:2007-2012. Pubmed: 8168497
  • Zapun, A., Missiakas, D., Raina, S., Creighton, T. E. (1995). "Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli." Biochemistry 34:5075-5089. Pubmed: 7536035