ATP synthase (proton-translocating ATPase) (EC 184.108.40.206) [1,2] is a component
of the cytoplasmic membrane of eubacteria, the inner membrane of mitochondria,
and the thylakoid membrane of chloroplasts. The ATPase complex is composed of
an oligomeric transmembrane sector, called CF(0), and a catalytic core, called
coupling factor CF(1). The former acts as a proton channel; the latter is
composed of five subunits, α, β, γ, delta and epsilon. Subunit
γ is believed to be important in regulating ATPase activity and the flow
of protons through the CF(0) complex. The best conserved region of the γ
subunit  is its C-terminus which seems to be essential for assembly and
catalysis. As a signature pattern to detect ATPase γ subunits, we used a
14 residue conserved segment where the last amino acid is found one to three
residues from the C-terminal extremity.
November 1995 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
Futai M. Noumi T. Maeda M.
ATP synthase (H+-ATPase): results by combined biochemical and molecular biological approaches.
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