PROSITE documentation PDOC00792PPM-type phosphatase domain signature and profile
Protein phosphatases remove phosphate groups from various proteins that are the key components of a number of signalling pathways in eukaryotes and prokaryotes. Protein phosphatases that dephosphorylate Ser and Thr residues are classified into the phosphoprotein (PPP) and the protein phosphatase Mg(2+)- or Mn(2+)-dependent (PPM) families. The core structure of PPMs is the 300-residue PPM-type phosphatase domain that catalyzes the dephosphorylation of phosphoserine- and phosphothreonine-containing protein. The PPM-type phosphatase domain is found as a module in diverse structural contexts and is modulated by targeting and regulatory subunits [1,2,3,4].
Some proteins known to contain a PPM-type phosphatase domain are listed below:
- Bacillus subtilis stage II sporulation protein E (SpoIIE), controls the sporulation by dephosphorylating an anti-transcription factor SpoIIAA, reversing the actions of the SpoIIAB protein kinase in a process that is gouverned by the ADP/ATP ratio [levdikov].
- Mycobacterium tuberculosis PP2C-family Ser/Thr phosphatase (PstP).
- Eucaryotic PP2C, a negative regulator of protein kinase cascades that are activated as a result of stress.
- Yeast adenyl cyclase, plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP.
- Mammalian mitochondrial pyruvate dehydrogenase phosphatase 1 (PDP1).
- Plant kinase-associated protein phosphatase (KAPP), regulates receptor-like kinase (RLK) signalling pathways.
- Plant absissic acid-insenstive 1 and 2 (ABI1 and ABI2), play a key absissic acid (ABA) signal transduction.
The PP2C-type phosphatase domain consists of 10 segments of β-strands and 5 segments of α-helix and comprises a pair of detached subdomains. The first is a small β-sandwich with strand β1 packed against strands β2 and β3; the second is a larger β-sandwich in which a four-stranded β-heet packs against a three-stranded β-sheet with flanking α-helices (see <PDB:3T9Q>) [1,3].
As a signature pattern, we selected the best conserved region which is located in the N-terminal part and contains a perfectly conserved tripeptide. This region includes a conserved aspartate residue involved in divalent cation binding [1]. We also developed a profile that covers the entire PPM-type phosphatase domain.
Last update:February 2015 / Text revised; profile added.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Das A.K. Helps N.R. Cohen P.T.W. Barford D. |
| Title | Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution. | |
| Source | EMBO J. 15:6798-6809(1996). | |
| PubMed ID | 9003755 |
| 2 | Authors | Rodriguez P.L. |
| Title | Protein phosphatase 2C (PP2C) function in higher plants. | |
| Source | Plant Mol. Biol. 38:919-927(1998). | |
| PubMed ID | 9869399 |
| 3 | Authors | Levdikov V.M. Blagova E.V. Rawlings A.E. Jameson K. Tunaley J. Hart D.J. Barak I. Wilkinson A.J. |
| Title | Structure of the phosphatase domain of the cell fate determinant SpoIIE from Bacillus subtilis. | |
| Source | J. Mol. Biol. 415:343-358(2012). | |
| PubMed ID | 22115775 | |
| DOI | 10.1016/j.jmb.2011.11.017 |
| 4 | Authors | Mori Y. Takegawa K. Kimura Y. |
| Title | Function analysis of conserved amino acid residues in a Mn(2+)-dependent protein phosphatase, Pph3, from Myxococcus xanthus. | |
| Source | J. Biochem. 152:269-274(2012). | |
| PubMed ID | 22668558 | |
| DOI | 10.1093/jb/mvs067 |
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