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sortase domain-bontaining protein
The founder member of this family is S. aureus sortase, a transpeptidase that attaches surface proteins by the threonine of an LPXTG motif to the cell wall [1]. [1]. 10427003. Staphylococcus aureus sortase, an enzyme that anchors surface. proteins to the cell wall.. Mazmanian SK, Liu G, Ton-That H, Schneewind O;. Science 1999;285:760-763.. [2]. 11239768. An embarrassment of sortases - a richness of substrates?. Pallen MJ, Lam AC, Antonio M, Dunbar K;. Trends Microbiol 2001;9:97-102. (from Pfam)
class A sortase SrtA
SrtA, as described originally in Staphylococcus aureus, is the founding member of the family of sortases, transpeptidases that occur almost exclusively in Gram-positive bacteria. Sortases cleave a recognition signal near the C-terminus of the target protein, usually an LPXTG-like sorting signal, and then reattach the protein so it becomes properly anchored. SrtA typically processes many proteins per proteome, attaching target proteins to a peptidoglycan precursor, so that the target protein becomes covalently attached to, and immobilized on, the cell surface. SrtA is classified as a class A sortase.
sortase
This family includes Staphylococcus aureus sortase A, a housekeeping transpeptidase that attaches surface proteins by the Thr of an LPXTG motif to the cell wall. The family also includes special purpose sortases required for correct assembly of LPXTG-containing fimbrial proteins. It excludes the sortase B family, for which the recognition site NPXTN is typical.
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