ATP Synthase Subunit C (atpE) Escherichia Coli Recombinant Protein

Function: F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. HAMAP-Rule MF_01396Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits. HAMAP-Rule MF_01396

Subunit structure: F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has three main subunits: a1, b2 and c(10). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Ref.12

Subcellular location: Cell inner membrane; Multi-pass membrane protein Ref.13.

Miscellaneous: Dicyclohexylcarbodiimide (DCDD) binding to the active aspartate residue inhibits ATPase in vitro. HAMAP-Rule MF_01396In this organism c-rings of between c8 and c(12) can be isolated in vivo following experimental manipulations, however only c8 and c9, in addition to c(10), are partially functional (Ref.12). HAMAP-Rule MF_01396

Sequence similarities: Belongs to the ATPase C chain family.