CydD functions as part of the CydDC transporter, which has two primary roles:
Thiol Export: Mediates ATP-dependent transport of cysteine and glutathione (GSH) to the periplasm, critical for cytochrome bd oxidase assembly .
Heme Regulation: Binds heme b and modulates ATPase activity, suggesting a regulatory role in redox homeostasis .
Key Functional Data:
Basal ATPase activity of purified CydDC: ~100 nmol Pi/min/mg .
Thiol compounds (e.g., cysteine) stimulate ATPase activity 3-fold; heme further enhances this activity but inhibits it at high concentrations .
Loss of CydD abolishes cytochrome bd assembly, confirmed by UV-Vis spectroscopy and oxygen consumption assays .
Cytochrome Restoration: Recombinant CydDC partially restores cytochrome bd assembly in cydD mutant strains, evidenced by regained heme d absorption at 650 nm .
Redox Homeostasis: cydD mutants exhibit defective periplasmic cytochrome c assembly, implicating CydDC in maintaining periplasmic redox balance .
Antibiotic Targets: Cytochrome bd (dependent on CydDC) is a target for antimicrobials like aurachin D, highlighting CydD’s pharmacological relevance .
Oxidative Stress: cydD mutants show heightened sensitivity to nitric oxide (NO), suggesting roles in pathogen resilience .
KEGG: ecj:JW0870
STRING: 316385.ECDH10B_0957