Mitochondrial membrane ATP synthase (F(1)F(o) ATP synthase) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:19436713, PubMed:29247468). F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(o) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:19436713, PubMed:29247468, PubMed:29440423). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1) (PubMed:19436713, PubMed:29440423). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (Probable). Contrary to the procyclic, insect form that requires F(1)F(o) ATP synthase for ATP synthesis, the bloodstream form relies on ATP hydrolysis by F(1)F(o) ATP synthase to maintain its mitochondrial membrane potential (PubMed:29247468). F-type ATPases have 2 components, F(1) - the catalytic core - and F(o) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1), plus the additional subunit P18 (Tb427.05.1710) that is not present in F(1)F(o) ATP synthase from metazoa (PubMed:19436713, PubMed:29247468, PubMed:29440423). Subunit P18 (Tb927.5.1710) interacts with the alpha subunit with a 1:1 stoichiometry; the interaction is direct (PubMed:29440423). Subunit gamma is part of the central stalk (PubMed:29440423). F(o) has three main subunits: a, b and c (PubMed:19436713). The trypanosomal ATPase complex contains additional subunits that are not present in the F(1)F(o) ATP synthase from metazoa (PubMed:19436713, PubMed:29247468, PubMed:29440423). RNAi-mediated knockdown of the protein impairs assembly of the F(1) component and slows the proliferation rate of procyclic cells that are cultivated in vitro in the presence of glucose. RNAi-mediated knockdown of the protein also slows the proliferation rate of the bloodstream form of the parasite, despite the fact that the organism can profit from blood glucose as source of energy. Mitochondrial membrane potential is dramatically reduced in the bloodstream form that relies on ATP hydrolysis to maintain mitochondrial membrane potential.