IPR017860
Peptidase M22, conserved site
InterPro entry
Short name | Peptidase_M22_CS |
Description
Glycoprotease (Gcp) (
3.4.24.57)
[1], or o-syaloglycoprotein endopeptidase, is a metalloprotease secreted by Pasteurella haemolytica which specifically cleaves O-sialoglycoproteins such as glycophorin A. It belongs to the peptidase family M22. The sequence of Gcp is highly similar to uncharacterised orthologues in most complete genomes of bacteria and archaebacteria as well as in yeast (QRI7 and YKR038c).
This entry represents a conserved site found in proteins classified as M22 peptidases, though there is a lack of experimental evidence to support peptidase activity as a general property of this family. This site contains two conserved histidines. It is possible that this region is involved in coordinating a metal ion such as zinc.
References
1.Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene. Abdullah KM, Lo RY, Mellors A. J. Bacteriol. 173, 5597-603, (1991). View articlePMID: 1885539
Cross References
Contributing Member Database Entry
- PROSITE patterns:PS01016