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- ************************************
- * ATP synthase a subunit signature *
- ************************************
-
- ATP synthase (proton-translocating ATPase) (EC 3.6.1.34) [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]-x-[STAG]-[LIVMF]-R-L-x-[SAGV]-N-[LIVM]
- [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: Azotobacter vinelandii nifA and a
- Eikenella corrodens hypothetical 66.3 Kd protein.
- -Last update: June 1992 / Pattern and text revised.
-
- [ 1] Futai M., Noumi T., Maeda M.
- Annu. Rev. Biochem. 58:111-136(1989).
- [ 2] Senior A.E.
- Physiol. Rev. 68:177-231(1988).
- [ 3] Lewis M.L., Chang J.A., Simoni R.D.
- J. Biol. Chem. 265:10541-10550(1990).
- [ 4] Cain B.D., Simoni R.D.
- J. Biol. Chem. 264:3292-3300(1989).
-