Secondary Evidence: Grauschopf,U., Winther,J.R., Korber,P., Zander,T., Dallinger,P. and Bardwell,J.C. Why is DsbA such an oxidizing disulfide catalyst? Cell. 83 (6), 947-955 (1995) PubMed: 8521518
Akiyama,Y., Kamitani,S., Kusukawa,N. and Ito,K. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product The Journal of biological chemistry. 267 (31), 22440-22445 (1992) PubMed: 1429594
Martin,J.L., Bardwell,J.C. and Kuriyan,J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo Nature. 365 (6445), 464-468 (1993) PubMed: 8413591
Guddat,L.W., Bardwell,J.C., Zander,T. and Martin,J.L. The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding Protein science : a publication of the Protein Society. 6 (6), 1148-1156 (1997) PubMed: 9194175
Comment: [FUNCTION] Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins. Involved in the production of protease and alkaline phosphatase, motility, metal resistance, and multi-drug resistance. [SUBCELLULAR LOCATION] Periplasmic (by similarity). [SIMILARITY] Belongs to the thioredoxin family. dsbA subfamily.
COGS Summary:COGS Search BeTs to 6 clades of COG0526 COG name: Thiol-disulfide isomerase and thioredoxins Functional Class: O,C The phylogenetic pattern of COG0526 is aompkzyqvdrlbcefghsnujxitw Number of proteins in this genome belonging to this COG is
Significant hit ( 6.3e-06) to 3/4 blocks of the IPB001853 family, which is described as "DSBA oxidoreductase". Interpro entry for IPR001853. IPB001853A 38-50 31 IPB001853B 66-80 81 IPB001853D 161-199 0.00092