F-class ATPases are primarily involved in:
F-type ATPases, often called ATP synthases, are evolutionarily related to V-type pumps but adapted for opposite physiological purpose in most contexts. Located in bacterial plasma membrane, mitochondrial inner membrane cristae and chloroplast thylakoid membrane, they consist of soluble F1 catalytic head containing alternating alpha and beta subunits around central gamma stalk and membrane embedded Fo base containing a subunit and c-ring proton channel. In respiring membranes electron transport complexes pump protons outward creating proton motive force combination of pH gradient and electrical potential about 200 millivolts. Protons re-enter through Fo c-ring causing rotation of c-ring and gamma which cyclically distorts beta subunits alternating among open, loose and tight states per Boyer's binding change mechanism, converting ADP plus inorganic phosphate into ATP. This mode uses reverse proton transport relative to typical pump direction, transforming electrochemical energy into chemical energy. ATP hydrolysis driven proton pumping occurs when gradient collapses, but principal cellular role remains synthesis not simply hydrolysis for ion transport.
Ref: Boyer, Nobel Lecture 1997, F-Type ATP Synthase Rotary Mechanism and ATP Synthesis.