GDSL lipase that catalyzes the hydrolysis of p-nitrophenyl (pNP) esters. pNP-decanoate (C10) is the preferred substrate. It can also use pNP-octanoate (C8), pNP-dodecanoate (C12) and pNP-tetradecanoate (C14). Has lower activity with pNP-butyrate (C4), pNP-palmitate (C16) and pNP-stearate (C18) (PubMed:31125644). Does not show phospholipase A1 activity (PubMed:31125644). Might help bacteria to utilize available lipids for its growth as well as provide resistance to various intracellular stresses by cell wall modulation resulting in enhanced intracellular survival (PubMed:31125644). a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol + H(+) decanoate ester + H2O = an aliphatic alcohol + decanoate + H(+) an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+) a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) + tetradecanoate Activity is inhibited by the serine modifier phenylmethylsulfonyl fluoride (PMSF). kcat is 14440 min(-1) with pNP-decanoate as substrate. Optimum pH is 9.0 (with pNP-decanoate as substrate). Optimum temperature is 40 degrees Celsius (with pNP-decanoate as substrate). Expression is up-regulated under nutrient starvation (in strain H37Ra). Expression in M.smegmatis alters colony morphology and growth kinetics, provides resistance to SDS, lysozyme and anti-TB drugs, increases the total lipid content and trehalose dimycolates, and enhances infection ability and intracellular survival capability of M.smegmatis. Belongs to the 'GDSL' lipolytic enzyme family.