v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Disulphide bonds contribute to folding, maturation, stability, and regulation of proteins, in particular those localized out of the cytosol. Oxidation of selected pairs of cysteines to disulphide in vivo requires cellular factors present in the bacterial periplasmic space or in the endoplasmic reticulum of eukaryotic cells [ , ].This family represents disulphide bond formation protein C (BdbC) from Bacillus subtilis which functionally corresponds to the well-characterised E. coli DsbB [ ]. |
| Short Name | Disulphide_bond_form_BdbC |