Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. PBP-2B is required for vegetative cell division and sporulation septation. Beta-lactamase inactivates the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis (Probable). This protein itself, but not its transpeptidase activity, is required for cell division (PubMed:28792086). Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. Cell wall biogenesis; peptidoglycan biosynthesis. Localizes at mid cell, to cell division sites; localization requires FtsZ. Synthesized throughout vegetative growth. Synthesis is enhanced during stage II of sporulation and in stage IV mother cells. Undetectable in stage IV forespores. Present in the inner forespore membrane of the dormant spore. Transcribed at a low constant level in all growth phases. Part of the mraZ-rsmH-ftsL-pbpB operon. Essential, it cannot be deleted (PubMed:8244929, PubMed:8636036). Depletion leads to an arrest of cell division after 80 minutes at 37 degrees Celsius and 40 minutes at 48 degrees Celsius with a concomitant reduction in FtsL and to a lesser extent DivIC levels; cells lengthen after arrest and eventually lyse (PubMed:16936019, PubMed:28792086). Belongs to the transpeptidase family. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus.