Catalyzes DD-carboxypeptidase and transpeptidation reactions. Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. Inhibited by cephaloridine. Optimum pH is 12. May be anchored in the membrane via a C-terminal amphipathic alpha helix. Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion (PubMed:20713508, PubMed:22882210). Expression starts at the end of the exponential phase and peaks two hours into sporulation. There is no enzyme activity in spores. Expression is sigma H-dependent. Belongs to the peptidase S13 family.