Cell-wall hydrolase that hydrolyzes the amide bond between N-acetylmuramic acid and L-alanine in cell-wall glycopeptides (PubMed:24311595, PubMed:24019530). Is able to hydrolyze the cell walls of several bacterial species (i.e. Paenibacillus sp., B.avium, E.coli DH5alpha, E.aerogenes, L.acidophilus, B.thuringiensis, B.pumilus, B.subtilis and E.coli W3110), thereby showing that it is a cell-wall hydrolase with broad-spectrum activity (PubMed:24311595). May have a role in peptidoglycan fragment recycling (PubMed:24019530). Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. The structure reveals a short flexible hairpin turn that partially occludes the active site and may be involved in autoregulation. Cell wall degradation; peptidoglycan degradation. Monomer. Disulfide oxidation is not required for folding of the enzyme core or in vitro muramyl dipeptide hydrolysis. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.