Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. 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). Rotation of the central stalk against the surrounding subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (Probable). Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). Binds the bacterial siderophore enterobactin and is required for the assimilation of enterobactin-bound iron from non-pathogenic bacteria. Promotes mitochondrial accumulation of enterobactin-derived iron ions (PubMed:30146159). Subunit of the F-type ATPase which has 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Ubiquitous (at protein level). RNAi-mediated knockdown of the protein leads to impaired growth and development. In addition, it impairs the assimilation of enterobactin-bound iron. The siderophore enterobactin (Ent) produced by enteric bacteria binds Fe(3+) and helps them scavenge iron ions from the environment. Enterobactin produced by non-pathogenic E.coli strains facilitates iron assimilation in C.elegans (PubMed:30146159). Other siderophores, such as ferrichrome and pyoverdine that is produced by pathogenic bacteria, do not facilitate intestinal iron absorption in C.elegans (PubMed:30146159). Belongs to the ATPase alpha/beta chains family.