The F₀F₁ ATP synthase in Bacillus species consists of two main components:
F₀: A membrane-bound proton channel (subunits a, b, c, and others).
F₁: A soluble catalytic domain (subunits α, β, γ, δ, ε).
AtpD encodes the β-subunit of F₀, which plays a structural role in proton translocation and ATP synthesis. In B. subtilis, atpD expression is linked to oxidative phosphorylation efficiency, with its deletion impairing ATP production . While B. cereus atpD-specific studies are absent in provided sources, its functional homology to B. subtilis atpD suggests analogous roles.
AtpD likely contributes to:
Oxidative phosphorylation: Generating ATP during aerobic respiration.
Stress responses: Acid resistance mechanisms, as shown by upregulation of F₁ ATP synthase subunits (e.g., atpB) during low-pH environments .
Redox regulation: Interactions with proteins like Rex, which modulates metabolic pathways in response to NADH/NAD⁺ ratios .
Recombinant atpD production involves heterologous expression systems (e.g., E. coli) for structural or functional studies. Such constructs enable:
Biochemical assays to measure proton translocation efficiency or ATP synthesis rates.
Proteomic analysis of stress-induced modifications (e.g., phosphorylation, redox-sensitive residues) .
KEGG: bcq:BCQ_5145