Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages. The synergistic effects on peptidoglycan degradation of RipA plus RpfB are inhibited by addition of PBP1A (ponA1). Optimum pH is between 5 and 5.5. Monomer. Interacts with RpfB and PBP1A (ponA1) via residues 448-472 of RipA, interacts with RpfE. Localizes to the septa upon expression in M.bovis or M.smegmatis. Remains associated with the cell. Was identified as a high-confidence drug target. Belongs to the peptidase C40 family. The role of the N-terminal domain is controversial. A recent paper (PubMed:21864539) found it had no effect on enzyme activity, while another (PubMed:20826344) reported that it had an inhibitory role and had to be cleaved off for full enzyme activity.