BdbC operates in tandem with BdbD (a DsbA homolog) to catalyze disulfide bond formation:
Oxidation Cycle:
Redox Potential:
BdbC mutations restore cytochrome c synthesis and sporulation in B. subtilis strains lacking CcdA, a thiol-reducing membrane protein .
This suppression highlights BdbC’s role in maintaining redox balance during post-translational modifications .
BdbC is essential for limiting secretion stress caused by disulfide bond-containing proteins like PhoA .
Example: bdbC mutants exhibit upregulated stress-response pathways (e.g., HtrA, HtrB proteases) .
Inactivation of bdbC abolishes genetic transformability by reducing ComGC stability, a competence protein requiring disulfide bonds .
PhoA Case Study: Co-expression of BdbC/BdbD enables B. subtilis to secrete active E. coli PhoA, which requires two disulfide bonds .
Yield Optimization: Overexpression of bdbC enhances oxidative folding capacity, improving yields of disulfide-bonded therapeutics (e.g., antibodies, cytokines) .
Advantages:
KEGG: bsu:BSU33470
STRING: 224308.Bsubs1_010100018171