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PROSITE documentation PDOC00139

P-type ATPases phosphorylation site





Description

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.

Last update:

November 2002 / Text revised.

Expert(s) to contact by email:

Axelsen K.B.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

ATPASE_E1_E2, PS00154; E1-E2 ATPases phosphorylation site  (PATTERN)


References

1AuthorsFagan M.J. Saier M.H. Jr.
TitleP-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees.
SourceJ. Mol. Evol. 38:57-99(1994).
PubMed ID8151716

2AuthorsPalmgren M.G. Axelsen K.B.
TitleEvolution of P-type ATPases.
SourceBiochim. Biophys. Acta 1365:37-45(1998).
PubMed ID9693719

3AuthorsAxelsen K.B. Palmgren M.G.
TitleEvolution of substrate specificities in the P-type ATPase superfamily.
SourceJ. Mol. Evol. 46:84-101(1998).
PubMed ID9419228



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