{PDOC00526} {PS00605; ATPASE_C} {BEGIN} ************************************ * ATP synthase c 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) c subunit (also called protein 9, proteolipid, or subunit III) [3,4] is a highly hydrophobic protein of about 8 Kd which has been implicated in the proton-conducting activity of ATPase. Structurally subunit c consist of two long terminal hydrophobic regions, which probably span the membrane, and a central hydrophilic region. N,N'-dicyclohexylcarbodiimide (DCCD) can bind covalently to subunit c and thereby abolish the ATPase activity. DCCD binds to a specific glutamate or aspartate residue which is located in the middle of the second hydrophobic region near the C-terminus of the protein. We derived a signature pattern which includes the DCCD-binding residue. -Consensus pattern: [GSTA]-R-[NQ]-P-x(5)-{A}-x-{F}-x(2)-[LIVMFYW](2)-x(3)- [LIVMFYW]-x-[DE] [D or E binds DCCD] -Sequences known to belong to this class detected by the pattern: ALL, except for sunflower mitochondrial encoded subunit C which has Trp instead of Arg in position 2 of the pattern. -Other sequence(s) detected in Swiss-Prot: 2. -Note: The proteolipid subunit of the vacuolar ATPase, a 16 Kd protein, which also binds DCCD, is evolutionary related to subunit c and has arisen by the duplication of a subunit c type domain. This protein is however too divergent to be detected by this pattern. -Last update: April 2006 / Pattern 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] Ivaschenko A.T., Karpenyuk T.A., Ponomarenko S.V. Biokhimiia 56:406-419(1991). [ 4] Recipon H., Perasso R., Adoutte A., Quetier F. "ATP synthase subunit c/III/9 gene sequences as a tool for interkingdom and metaphytes molecular phylogenies." J. Mol. Evol. 34:292-303(1992). PubMed=1533253 -------------------------------------------------------------------------------- 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}