Homologous Superfamily

Disulphide bond isomerase, DsbC, N-terminal (IPR009094)

Short name: DiS-bond_isomerase_DsbC_N

Overlapping entries


The disulphide bond isomerase (DsbC) is one of five Escherichia coli proteins required for disulphide bond formation, and functions to rearrange incorrect disulphide bonds during oxidative protein folding in the periplasm. DsbC acts as a homodimer with both disulphide isomerase and chaperone activity. It is selectively activated by the transmembrane electron transporter DsbDalpha, which functions as a thiol oxireductase [PMID: 12234918]. Like other Dsb proteins, DsbC contains active site Cys-X-X-Cys sequences that form disulphide bonds, characteristic of thioredoxin proteins. DbsC consists of thioredoxin-like domains joined by a flexible hinge region to an N-terminal dimerisation domain. The crystal structure of the N-terminal domain reveals an alpha-beta(4) core, where the helix packs against the coiled antiparallel beta-sheet [PMID: 10700276].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.