************************************** * E1-E2 ATPases phosphorylation site * ************************************** E1-E2 ATPases are cation transport ATPases which form an aspartyl phosphate intermediate in the course of ATP hydrolysis. ATPases which belong to this family are listed below [1,2,3]. - Fungal and plant plasma membrane (H+) ATPases [reviewed in 3]. - Vertebrate (Na+, K+) ATPases (sodium pump) [reviewed in 5,6]. - Gastric (K+, H+) ATPases (proton pump). - Calcium (Ca++) ATPases (calcium pump) from the sarcoplasmic reticulum (SR), the endoplasmic reticulum (ER) and the plasma membrane. - Copper (Cu++) ATPases (copper pump) which are involved in two human genetic disorders: Menkes syndrome and Wilson disease [7]. - Bacterial potassium (K+) ATPases. - Bacterial cadmium efflux (Cd++) ATPases [reviewed in 8]. - Bacterial magnesium (Mg++) ATPases [9]. - A probable cation ATPase from Leishmania. - fixI, a probable cation ATPase from Rhizobium meliloti, involved in nitrogen fixation. The region around the phosphorylated aspartate residue is perfectly conserved in all these ATPases and can be used as a signature pattern. -Consensus pattern: D-K-T-G-T-[LIVM]-[TI] [D is phosphorylated] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in SWISS-PROT: Staphylococcus aureus DNA gyrase subunit B. -Last update: June 1994 / Pattern and text revised. [ 1] Green N.M., McLennan D.H. Biochem. Soc. Trans. 17:819-822(1989). [ 2] Green N.M. Biochem. Soc. Trans. 17:970-972(1989). [ 3] Fagan M.j., Saier M.H. Jr. J. Mol. Evol. 38:57-99(1994). [ 4] Serrano R. Biochim. Biophys. Acta 947:1-28(1988). [ 5] Fambrough D.M. Trends Neurosci. 11:325-328(1988). [ 6] Sweadner K.J. Biochim. Biophys. Acta 988:185-220(1989). [ 7] Bull P.C., Thomas G.R., Rommens J.M., Forbes J.R., Cox D. Nature Genet. 5:327-337(1993). [ 8] Silver S., Nucifora G., Chu L., Misra T.K. Trends Biochem. Sci. 14:76-80(1989). [ 9] Snavely M.D., Miller C.G., Maguire M.E. J. Biol. Chem. 266:815-823(1991).