 |
|
| 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.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
| ATPASE_E1_E2, PS00154; E1-E2 ATPases phosphorylation site (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: |
1 |
|
|
|
| Matching PDB structures:
1FQU 1IWO 1KJU 1MHS ... [ALL] |
References:
| 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 |
Copyright:
PROSITE is copyright. It is produced by the Swiss Institute of
Bioinformatics (SIB). There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to license@isb-sib.ch or
see: http://www.expasy.org/prosite/prosite_license.htm.
Miscellaneous:
View entry in original PROSITE document format
View entry in raw text format (no links)