{PDOC00420} {PS00449; ATPASE_A} {BEGIN} ************************************ * ATP synthase a subunit signature * ************************************ ATP synthase (proton-translocating ATPase) (EC 3.6.3.14) [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), which acts as a proton channel, and a catalytic core, termed coupling factor CF(1). The CF(0) a subunit, also called protein 6, is a key component of the proton channel; it may play a direct role in translocating protons across the membrane. It is a highly hydrophobic protein that has been predicted to contain 8 transmembrane regions [3]. Sequence comparison of a subunits from all available sources reveals very few conserved regions. The best conserved region is located in what is predicted to be the fifth transmembrane domain. This region contains three perfectly conserved residues: an arginine, a leucine and an asparagine. Mutagenesis experiments carried out in Escherichia coli [4] have shown that the arginine is necessary for proton translocation and that its replacement by another amino acid results in loss of ATPase activity. We selected this region as a signature pattern. -Consensus pattern: [STAGN]-{E}-[STAG]-[LIVMF]-R-L-{LP}-[SAGV]-N-[LIVMT] [R is important for proton translocation] -Sequences known to belong to this class detected by the pattern: ALL, except for the Mytilus edulis and Trypanosoma brucei subunits. -Other sequence(s) detected in Swiss-Prot: 8. -Last update: December 2004 / Pattern and text revised. [ 1] Futai M., Noumi T., Maeda M. "ATP synthase (H+-ATPase): results by combined biochemical and molecular biological approaches." Annu. Rev. Biochem. 58:111-136(1989). PubMed=2528322; DOI=10.1146/annurev.bi.58.070189.000551 [ 2] Senior A.E. "ATP synthesis by oxidative phosphorylation." Physiol. Rev. 68:177-231(1988). PubMed=2892214 [ 3] Lewis M.J., Chang J.A., Simoni R.D. "A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments." J. Biol. Chem. 265:10541-10550(1990). PubMed=2162353 [ 4] Cain B.D., Simoni R.D. "Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit." J. Biol. Chem. 264:3292-3300(1989). PubMed=2536742 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}