May function as a peptidoglycan hydrolase with glycosidase activity (PubMed:25260828). In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4) (PubMed:25869294). Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Optimum pH is 8.0 for the hydrolysis of p-nitrophenyl butyrate. Optimum temperature is 38 degrees Celsius for the hydrolysis of p-nitrophenyl butyrate. Cell wall degradation; peptidoglycan degradation. Upon exposure to antituberculous drugs such as isoniazid, ethionamide or PA-824, Rv2525c expression is significantly up-regulated together with those of other genes involved in cell wall processes. Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. Cells lacking this gene display an increase in susceptibility to some beta-lactam antibiotics and, despite slower growth in vitro, enhanced virulence in both cellular and murine models of tuberculosis. No detectable difference in the lipid profiles.