PROSITE documentation PDOC00139

P-type ATPases (also known as E1-E2) 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 (EC 3.6.3.6).
Vertebrate (Na+, K+) ATPases (sodium pump) (EC 3.6.3.9).
Gastric (K+, H+) ATPases (proton pump) (EC 3.6.3.10).
Calcium (Ca++) ATPases (calcium pump) (EC 3.6.3.8) from the sarcoplasmic reticulum (SR), the endoplasmic reticulum (ER) and the plasma membrane.
Copper (Cu++) ATPases (copper pump) (EC 3.6.3.4) which are involved in two human genetic disorders: Menkes syndrome and Wilson disease.
Bacterial cadmium efflux (Cd++) ATPases (EC 3.6.3.3).
Bacterial magnesium (Mg++) ATPases (EC 3.6.3.2).
Bacterial potassium (K+) ATPases (EC 3.6.3.12).
Bacterial zinc (Zn+) ATPases (EC 3.6.3.5).
Fungal ENA sodium ATPases (EC 3.6.3.7).
fixI, a probable cation ATPase from Rhizobacea, 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.

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1	Authors	Fagan M.J., Saier M.H. Jr.
	Title	P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees.
	Source	J. Mol. Evol. 38:57-99(1994).
	PubMed ID	8151716

2	Authors	Palmgren M.G., Axelsen K.B.
	Title	Evolution of P-type ATPases.
	Source	Biochim. Biophys. Acta 1365:37-45(1998).
	PubMed ID	9693719

3	Authors	Axelsen K.B., Palmgren M.G.
	Title	Evolution of substrate specificities in the P-type ATPase superfamily.
	Source	J. Mol. Evol. 46:84-101(1998).
	PubMed ID	9419228

P-type ATPases phosphorylation site

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