Hydrolyzes short-chain esters. Shows maximal activity with triacetin and p-nitrophenyl acetate. Has no enzyme activity on triacylglycerides or p-nitrophenyl esters (p-NP) with long fatty acids (tricaprin, p-NP caprylate, or p-NP caprate); experiments performed with enzyme missing the first 97 residues (PubMed:15939293). Has phospholipase C activity, making 1,2-DAG phosphocholine; experiments performed with enzyme missing the first 97 residues (PubMed:18535356). a carboxylic ester + H2O = a carboxylate + an alcohol + H(+) a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine kcat is 581.2 sec(-1) for triacetin. kcat is 223.7 sec(-1) for tributyrin. kcat is 122.9 sec(-1) for tricaproin. kcat is 15.6 sec(-1) for tricaprylin. kcat is 501.8 sec(-1) for p-nitrophenyl acetate. kcat is 119.7 sec(-1) for p-nitrophenyl butyrate. kcat is 33.1 sec(-1) for p-nitrophenyl caproate. Optimum pH is 7.5. Optimum temperature is 35 degrees Celsius. Detected by antibodies in a wild-type strain and upon expression of a probably truncated form in M.smegmatis. Induced by acidic pH. Mutants show reduced ability to grow in a mouse lung. Belongs to the 'GDXG' lipolytic enzyme family. Experiments to characterize enzymatic activity in (PubMed:21969609) and (PubMed:10564470) were performed with protein overexpressed in E.coli or M.smegmatis respectively; both papers use a protein that starts on Val-97 (PubMed:15939293, PubMed:18535356). Three start sites have been proposed for this protein, Met-1, Met-47 and Val-97, this is the longest translation. There is protein sequence that suggests Met-1 is the correct start. Antibodies detect a protein larger than 38 kDa in M.tuberculosis (PubMed:18535356). Truncated N-terminus.