Transpeptidase that anchors surface proteins to the cell wall (Probable) (PubMed:16247833, PubMed:19129190). 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). Catalyzes a cell wall sorting reaction in which a surface protein with the consensus sorting signal NP(Q/K)(T/S)(N/G/S)(D/A) is cleaved between the fourth and fifth residues, and the fourth position is linked to the cell wall (Probable) (PubMed:19129190). This is not the major sortase in Listeria, it seems to anchor only 2 proteins, Hbp2 (SvpA) and Hbp1 (PubMed:15028680, PubMed:16247833). Strongly expressed in mid-log phase, cotranscribed with lmo2182 and lmo2180, the sixth gene in a possible lmo2186-lmo2180 operon (PubMed:15028680). Induced under iron-deficient conditions and when fur (lmo1956, AC Q8Y5U9) is deleted (Probable). Induced when bacteria are grown in human cell lines (Probable). Decreased hemin-binding and hemin uptake by whole bacteria (PubMed:21545655). No visible phenotype in growth, no change in cell wall-anchoring of InlA, no effect on bacterial growth within host cells nor on virulence in a mouse infection model (PubMed:15028680). Loss of cell wall-anchoring of Hbp2 (SvpA); Hbp2 is still secreted and runs with an apparent lower molecular weight in gels (PubMed:15028680). A double srtA-srtB deletion mutant has no cell wall-anchored proteins (PubMed:15028680). No cell wall anchoring of Hbp1 or Hbp2 (SvpA) (PubMed:16247833). Does not impair iron transport (PubMed:15661014, PubMed:16430693). Decreased binding and uptake of hemin at low (0.5 uM and 5 uM) but not high hemin concentrations (at 50 uM no effect is seen) (PubMed:21545655). Belongs to the bacterial sortase family. Class B subfamily.