TesA is a multifunctional esterase that can act as a thioesterase, lysophospholipase and protease (PubMed:8098033, PubMed:8432696, PubMed:1864840, PubMed:4945109, PubMed:4554913, PubMed:238979, PubMed:791643, PubMed:8132479, PubMed:9070299, PubMed:10423542). TesA functions as a thioesterase specific for fatty acyl thioesters of greater than ten carbons, with highest activity on palmitoyl-CoA, cis-vaccenoyl-CoA and palmitoleoyl-CoA (PubMed:8098033, PubMed:4554913, PubMed:8132479, PubMed:9070299, PubMed:10423542). TesA also possesses an arylesterase activity towards short acyl-chain aromatic esters such as alpha-naphthyl acetate, alpha-naphthyl butyrate, benzyl acetate and phenyl acetate (PubMed:9070299). Also able to hydrolyze short acyl-chain triacylglycerols such as triacetin and tributyrin, and p-nitrophenyl esters such as p-nitrophenyl hexanoate and p-nitrophenyl butyrate (PubMed:9070299). The protease activity is mainly active on small peptides (PubMed:8432696, PubMed:9070299). TesA is also able to hydrolyze p-nitrophenyl esters of N-substituted amino acids such as N-benzyloxycarbonyl-L-Phe-p-nitrophenyl ester (Z-L-Phe-ONp) and N-benzyloxycarbonyl-L-Tyr-p-nitrophenyl ester (Z-L-Tyr-ONp), however it is unable to hydrolyze N-acetyl-L-Phe ethyl ester and its Tyr analog (PubMed:8432696, PubMed:791643, PubMed:10423542). TesA also hydrolyzes N-benzyloxycarbonyl-L-Phe beta-nitrophenyl ester (Cbz-Phe-ONap) and N-acetyl-DL-Phe-2-naphthyl ester (chymotrypsin-like specificity) (PubMed:8432696, PubMed:4945109). Shows a slow proteolytic activity against denatured casein (PubMed:4945109). The lysophospholipase activity of TesA is able to hydrolyze 1-palmitoyl-sn-glycero-3-phosphocholine, 1-acyl-sn-glycero-3-phosphoglycerol, 1- and 2-acyl-sn-glycero-3-phosphoethanolamine (PubMed:1864840, PubMed:238979, PubMed:10423542). a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+) H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate (9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+) H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate (9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+) (9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP] (11Z)-octadecenoyl-CoA + H2O = (11Z)-octadecenoate + CoA + H(+) H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA + H(+) dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+) decanoyl-CoA + H2O = CoA + decanoate + H(+) H2O + hexanoyl-CoA = CoA + H(+) + hexanoate a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine a phenyl acetate + H2O = a phenol + acetate + H(+) a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+) a hexanoate ester + H2O = an aliphatic alcohol + H(+) + hexanoate an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate Thioesterase activity is inhibited by iodoacetamide and photoactivated methylene blue, and slowly inhibited by 2,4-dinitrofluorobenzene (PubMed:4554913). Protease and lysophospholipase activities are inhibited by diisopropylfluorophosphate (DFP) (PubMed:1864840, PubMed:4945109, PubMed:238979). Lysophospholipase activity is inhibited by Fe(2+), Fe(3+) and Al(3+) ions (PubMed:238979). Diethyl p-nitrophenyl phosphate (DENP) irreversibly inhibits both the protease and thioesterase activities (PubMed:12846577). kcat is 88.99 sec(-1) for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate (PubMed:16515533). kcat is 62.4 sec(-1) for p-nitrophenyl butyrate as substrate (PubMed:9070299). kcat is 15.29 sec(-1) for p-nitrophenyl butyrate as substrate (PubMed:16515533). kcat is 14.1 sec(-1) for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate (PubMed:9070299). kcat is 10.13 sec(-1) for lauroyl-CoA as substrate (PubMed:16515533). kcat is 5.1 sec(-1) for p-nitrophenyl decanoate as substrate (PubMed:9070299). kcat is 2.6 sec(-1) for palmitoyl-CoA as substrate (PubMed:9070299). kcat is 2.3 sec(-1) for N-benzyloxycarbonyl-D-tyrosine-p-nitrophenyl ester as substrate (PubMed:9070299). Optimum pH is 7.5-8.4 (PubMed:4945109, PubMed:4554913, PubMed:12846577). Stable between pH 6.1 and 12, however, below pH 6.0, thioesterase rapidly loses activity (PubMed:4554913). Protease is stable up to 50 degrees Celsius. Monomer or homotetramer. Cells lacking this gene do not show thioesterase activity and have a little protease activity against Cbz-Phe-ONap. No effect on the cell growth and fatty acid composition. Belongs to the 'GDSL' lipolytic enzyme family. Extended N-terminus.