Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis (By similarity). As a bacterial surface-associated protein, mediates attachment to polystyrene surfaces, contributing to biofilm formation. Has also vitronectin-binding activity. Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein, the rest of the oligosaccharide is released intact. Oligomer; forms a ring structure at the cell surface which is important for efficient partitioning of daughter cells after cell division. Secreted, and then anchored on the cell surface at the peripheral cell wall above the completed septum (septal region), for the next cell division cycle. The GW domains are responsible for directing the proteins to the septal region. Undergoes proteolytic processing to generate the two extracellular lytic enzymes, probably at the septal region on the cell surface. In the N-terminal section; belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. In the C-terminal section; belongs to the glycosyl hydrolase 73 family.