Amidase hydrolyzing N-acetylmuramyl-L-Ala bond of MurNAc peptides; Involved in muropeptide recycling. Hydrolyzes the amide bond between N-acetylmuramic acid (MurNAc) and the L-alanine residue of the stem peptide. Cannot hydrolyze muropeptides containing N- acetylglucosamine (GlcNAc) at the non-reducing end.

D-lactyl ether N-acetylmuramic-6-phosphate acid etherase; Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D- lactate.

Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator.

Exported N-acetylglucosaminidase (major autolysin) (CWBP90); Cell wall hydrolase not involved in cell autolysis, competence, sporulation or germination. It hydrolyzes the beta-1,4 glycan bond between the N-acetylglucosaminyl and the N-acetylmuramoyl residues in the glycan chain.

Exoglucosaminidase; Is the major glucosaminidase responsible for peptidoglycan structural determination during vegetative growth. Catalyzes the hydrolysis of 1,4-beta-linkages between N-acetyl-D-glucosamine and N- acetylmuramic acid residues in peptidoglycan. Acts processively from the ends of the glycan strands. Also plays a role in motility, chemotaxis and cell division.

Muropeptide L,D-carboxypeptidase; May be involved in the degradation of peptidoglycan by catalyzing the cleavage of the terminal D-alanine residue from cytoplasmic murein peptides; Belongs to the peptidase S66 family.

Putative PTS system EIIBC component ybbF; The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane.

Putative undecaprenyl-phosphate N-acetylgalactosaminyl-1-phosphate transferase; Autolysins are cell wall hydrolases involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. Has a high affinity for teichoic acid-endowed peptidoglycan. LytC is required for efficient swarming motility but not at the level of cell separation or flagellum biosynthesis. Rather, LytC appears to be important for proper flagellar function.

Sporulation-specific L-Ala-D-Glu endopeptidase; L-Ala--D-Glu endopeptidase involved in production of single L-alanine side chains from tetrapeptides in the spore cortex peptidoglycan. Therefore, is required for the endospore cortex maturation.