|PROSITE documentation PDOC00779|
Glycoprotease (GCP) (EC 220.127.116.11) , or o-syaloglycoprotein endopeptidase, is a metalloprotease secreted by Pasteurella haemolytica which specifically cleaves O-sialoglycoproteins such as glycophorin A. The sequence of GCP is highly similar to uncharacterized orthologs in most complete genomes of bacteria and archaebacteria as well as in yeast (QRI7 and YKR038c).
One of the conserved regions contains two conserved histidines. It is possible that this region is involved in coordinating a metal ion such as zinc.Note:
April 2006 / Pattern revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Abdullah K.M., Lo R.Y.C., Mellors A.|
|Title||Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene.|
|Source||J. Bacteriol. 173:5597-5603(1991).|
|2||Authors||Rawlings N.D., Barrett A.J.|
|Title||Evolutionary families of metallopeptidases.|
|Source||Methods Enzymol. 248:183-228(1995).|