The ATP synthase of Heliobacterium modesticaldum, a thermophilic anaerobic phototrophic bacterium, is an F-type rotary nanomachine critical for energy conversion. This enzyme comprises a hydrophilic F subcomplex (αβγδε) and a hydrophobic F subcomplex (a, b, c) . The δ subunit (encoded by atpH) is part of the peripheral stalk connecting F and F, playing a structural and regulatory role in coupling proton translocation to ATP synthesis .
Gene cluster: The ATP synthase operon in H. modesticaldum includes atpH alongside other subunits (α, β, γ, ε, a, b, c) .
Functional role: The δ subunit ensures efficient energy coupling during phototrophic growth, which is critical given the bacterium’s reliance on cyclic electron transport for ATP synthesis .
The δ subunit co-purifies with the holoenzyme using:
Detergent solubilization: β-DDM and OG maintain enzyme integrity .
Sucrose density gradient centrifugation: Isolates intact FF complexes .
Western blotting: Polyclonal antibodies confirm subunit identity .
Despite successful native purification, recombinant production of δ remains unreported. Heterologous systems (e.g., E. coli) used for related Firmicutes could be adapted, leveraging vectors like pAL95R with cbp2 or eno promoters .
KEGG: hmo:HM1_1101
STRING: 498761.HM1_1101