Transpeptidase that anchors surface proteins to the cell wall (PubMed:15968076). 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 (PubMed:15968076). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:15968076). Important for growth in macrophages. May be critical in the early stages of inhalation anthrax (PubMed:16041044). Inhibited by thiol-reactive reagents. Expressed in vegetative cells. Contains a unique N-terminal appendage positioned within the active site and in contact with catalytically essential histidine residue (PubMed:20489200). This appendage modulates substrate access to the enzyme. It may increase the efficiency of protein display by reducing the unproductive hydrolytic cleavage of enzyme-protein covalent intermediates that form during the cell wall anchoring reaction (PubMed:26324714). Disruption of the gene results in dramatic attenuation of the growth of the bacteria within J774A.1 cells, a mouse macrophage-like cell line (PubMed:16041044). Disruption does not affect the development of acute anthrax disease in the A/J mouse model (PubMed:15968076). Belongs to the bacterial sortase family. Class A subfamily.