Gene Name: qoxA (SE_0759 in some strains)
Synonyms: Quinol oxidase polypeptide II, Probable quinol oxidase subunit 2 .
UniProt IDs: Q5HQA9 (full-length) , Q8CPP6 (partial) , Q8CMQ2 (partial) .
Sequence Length:
The protein contains a His-tag (N-terminal in recombinant versions) and shares structural homology with quinol oxidase subunits in other Gram-positive bacteria.
Recombinant qoxA is produced in:
qoxA is a subunit of a cytochrome bd-type quinol oxidase, which catalyzes electron transfer from quinols to oxygen in the ETC . This enzyme is critical for:
Aerobic respiration: Under oxic conditions, it supports bacterial growth and biofilm formation .
Oxygen adaptation: Regulated by the SrrAB two-component system, which modulates qoxBACD operon expression (including qoxA) in response to oxygen levels .
SrrAB dependency: SrrAB upregulates qoxBACD under oxic conditions, linking qoxA expression to electron transport efficiency and biofilm maturation .
Metabolic adaptation: qoxA activity is coupled with fermentation pathways (e.g., pflBA) under microaerobic conditions, enabling survival in diverse niches .
ELISA kits: Recombinant qoxA is used as an antigen to detect anti-S. epidermidis antibodies .
Western blotting: Validates protein expression in S. epidermidis mutants or clinical isolates .
Biofilm regulation: qoxA knockout models investigate its role in oxygen-dependent biofilm formation .
Protein-protein interactions: Studies explore SrrAB binding to qoxA promoter regions .
Oxic conditions: SrrAB activates qoxBACD (including qoxA) to enhance ETC activity and biofilm production .
Microaerobic conditions: SrrAB downregulates qoxA while upregulating fermentation genes (e.g., pflBA) .
Pathogenicity: qoxA is expressed in both commensal and pathogenic S. epidermidis strains, though its role in virulence remains unclear .
Antibiotic resistance: Horizontal gene transfer of mecA (methicillin resistance) in S. epidermidis populations may intersect with qoxA-related metabolic pathways .
KEGG: ser:SERP0646
STRING: 176279.SERP0646