Transpeptidase that anchors surface proteins to the cell wall (PubMed:11854224, PubMed:11929538, PubMed:16247833, PubMed:22837151). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (Probable). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:11929538). Involved in pathogenesis (PubMed:11854224, PubMed:11929538, PubMed:15028680). May regulate the rate of synthesis and/or the stability of a subset of LPXTG proteins (PubMed:22837151). Not involved in cell wall-anchoring of Hbp2 (SvpA) or Hbp1 (PubMed:15028680, PubMed:16247833).

Belongs to the bacterial sortase family. Class A subfamily.

222 amino acids

MLKKTIAIIILIIGLLLIFSPFIKNGIVKYMSGHETIEQYKASDIKKNNEKDATFDFESVQLPSMTSVIKGAANYDKDAVVGSIAVPSVDVNLLVFKGTNTANLLAGATTMRSDQVMGKGNYPLAGHHMRDESMLFGPIMKVKKGDKIYLTDLENLYEYTVTETKTIDETEVSVIDNTKDARITLITCDKPTETTKRFVAVGELEKTEKLTKELENKYFPSK

24.7 kDa

(Note: Representative image - actual molecular weight may vary depending on tag type and expression method)

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