Required for efficient cell division, cell polarity and normal cell morphology (PubMed:20497504, PubMed:20497503, PubMed:20497502). Facilitates remodeling of the peptidoglycan layer and, thus, coordinated constriction of the cell envelope during the division process (PubMed:20497502, PubMed:20497504). Plays a critical role in maintaining proper cell envelope architecture during growth and division (PubMed:20497504). Required for normal envelope invagination during cell division and to establish or maintain outer membrane connections throughout the cell envelope (PubMed:20497504). May serve as a regulatory hub coordinating the activities of multiple peptidoglycan-degrading enzymes during cell constriction. Required to position SdpA and SdpB at midcell (PubMed:28833791). Localizes to the division site in an FtsZ-dependent manner during early stages of the division process (PubMed:20497504, PubMed:20497503, PubMed:20497502). Localization also depends on FtsN (PubMed:20497502). Composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. The LysM domains are the major mediators of the localization to the division site, probably via direct interaction with peptidoglycans. The LytM region is dispensable for localization, but is essential for function. Deletion mutant exhibits morphological defects, including cell widening and filamentation, and cell division defects (PubMed:20497504, PubMed:20497503, PubMed:20497502). Inactivation causes severe defects in outer membrane invagination, resulting in a significant delay between cytoplasmic compartmentalization and final separation of the daughter cells (PubMed:20497502). Cells lacking the gene also show outer membrane blebbing at the division site, at cell poles and along the cell body (PubMed:20497504).