Exhibits lipolytic activity with medium chain length esters as optimum substrates (PubMed:30560095). In vitro, pNP-caprylate (C8) is the optimum substrate followed by pNP-capricate (C10) (PubMed:30560095). May modulate the cell wall lipids to favor the survival of bacteria under stress conditions (PubMed:30560095). a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol + H(+) an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate decanoate ester + H2O = an aliphatic alcohol + decanoate + H(+) a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+) a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+) an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+) a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) + tetradecanoate kcat is 2 min(-1) with pNP-caprylate as substrate. Optimum pH is 9.0. Optimum temperature is 45 degrees Celsius. Cell wall anchored. Binds peptidoglycans via the LytM domains. Expression is up-regulated under nutrient depletion condition. Contains an N-terminal LytE region, which consists of three consecutive LysM domains, and a C-terminal esterase domain. LytM domains are essential for anchoring protein to the cell wall. The presence of LytM domains results in enhanced rate of protein aggregation at higher temperature. Overexpression in M.smegmatis leads to change in colony morphology, enhanced pellicle and aggregate formation, which may be linked with the changed lipid composition of the cell wall. Cell wall has higher amount of lipids, with a significant increase in trehalose dimycolate content. Overexpression also leads to increased drug resistance and enhanced intracellular survival inside the macrophage cell line. Belongs to the AB hydrolase superfamily.