ID TESA_ECOLI Reviewed; 208 AA. AC P0ADA1; P29679; P37331; P77125; Q2MBT3; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Thioesterase 1/protease 1/lysophospholipase L1 {ECO:0000303|PubMed:15697222}; DE Short=TAP {ECO:0000303|PubMed:15697222}; DE AltName: Full=Acyl-CoA thioesterase 1 {ECO:0000303|PubMed:8098033}; DE Short=TESA {ECO:0000303|PubMed:8098033}; DE EC=3.1.2.2 {ECO:0000269|PubMed:4554913}; DE AltName: Full=Acyl-CoA thioesterase I {ECO:0000303|PubMed:8098033}; DE AltName: Full=Arylesterase {ECO:0000303|PubMed:9070299}; DE EC=3.1.1.2 {ECO:0000269|PubMed:9070299}; DE AltName: Full=Lysophospholipase L1 {ECO:0000303|PubMed:1864840}; DE EC=3.1.1.5 {ECO:0000305|PubMed:10423542, ECO:0000305|PubMed:1864840}; DE AltName: Full=Oleoyl-[acyl-carrier-protein] hydrolase {ECO:0000303|PubMed:4554913}; DE EC=3.1.2.14 {ECO:0000269|PubMed:4554913}; DE AltName: Full=Phospholipid degradation C {ECO:0000303|PubMed:1864840}; DE Short=Pldc {ECO:0000303|PubMed:1864840}; DE AltName: Full=Protease 1 {ECO:0000303|PubMed:4945109}; DE EC=3.4.21.- {ECO:0000305|PubMed:791643}; DE AltName: Full=Protease I {ECO:0000303|PubMed:4945109}; DE AltName: Full=Thioesterase I/protease I {ECO:0000303|PubMed:12846577}; DE Short=TEP-I {ECO:0000303|PubMed:12846577}; DE Flags: Precursor; GN Name=tesA {ECO:0000303|PubMed:8098033}; GN Synonyms=apeA {ECO:0000303|PubMed:8432696}, pldC GN {ECO:0000303|PubMed:1864840}; OrderedLocusNames=b0494, JW0483; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION RP AS A THIOESTERASE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, ACTIVE SITE, RP SUBUNIT, AND NOMENCLATURE. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8098033; DOI=10.1016/s0021-9258(18)98341-9; RA Cho H., Cronan J.E. Jr.; RT "Escherichia coli thioesterase I, molecular cloning and sequencing of the RT structural gene and identification as a periplasmic enzyme."; RL J. Biol. Chem. 268:9238-9245(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-38, FUNCTION AS A RP PROTEASE, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, SUBSTRATE RP SPECIFICITY, AND NOMENCLATURE. RC STRAIN=K12; RX PubMed=8432696; DOI=10.1128/jb.175.4.1032-1037.1993; RA Ichihara S., Matsubara Y., Kato C., Akasaka K., Mizushima S.; RT "Molecular cloning, sequencing, and mapping of the gene encoding protease I RT and characterization of proteinase and proteinase-defective Escherichia RT coli mutants."; RL J. Bacteriol. 175:1032-1037(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP PROTEIN SEQUENCE OF 27-37, FUNCTION AS A LYSOPHOSPHOLIPASE, CATALYTIC RP ACTIVITY, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT, AND RP NOMENCLATURE. RC STRAIN=K12; RX PubMed=1864840; RA Karasawa K., Kudo I., Kobayashi T., Homma H., Chiba N., Mizushima H., RA Inoue K., Nojima S.; RT "Lysophospholipase L1 from Escherichia coli K-12 overproducer."; RL J. Biochem. 109:288-293(1991). RN [7] RP FUNCTION AS A PROTEASE, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY RP REGULATION. RX PubMed=4945109; DOI=10.1111/j.1432-1033.1971.tb01638.x; RA Pacaud M., Uriel J.; RT "Isolation and some propeties of a proteolytic enzyme from Escherichia coli RT (protease I)."; RL Eur. J. Biochem. 23:435-442(1971). RN [8] RP FUNCTION AS A THIOESTERASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT. RX PubMed=4554913; DOI=10.1016/s0021-9258(19)45222-8; RA Bonner W.M., Bloch K.; RT "Purification and properties of fatty acyl thioesterase I from Escherichia RT coli."; RL J. Biol. Chem. 247:3123-3133(1972). RN [9] RP FUNCTION AS A LYSOPHOSPHOLIPASE, ACTIVITY REGULATION, AND SUBSTRATE RP SPECIFICITY. RX PubMed=238979; DOI=10.1016/s0021-9258(19)41297-0; RA Doi O., Nojima S.; RT "Lysophospholipase of Escherichia coli."; RL J. Biol. Chem. 250:5208-5214(1975). RN [10] RP FUNCTION AS A PROTEASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBSTRATE SPECIFICITY, AND SUBUNIT. RX PubMed=791643; DOI=10.1111/j.1432-1033.1976.tb10867.x; RA Pacaud M., Sibilli S., Bras G.; RT "Protease I from Escherichia coli. Some physicochemical properties and RT substrate specificity."; RL Eur. J. Biochem. 69:141-151(1976). RN [11] RP FUNCTION AS A THIOESTERASE, AND SUBSTRATE SPECIFICITY. RX PubMed=8132479; DOI=10.1128/jb.176.6.1793-1795.1994; RA Cho H., Cronan J.E. Jr.; RT "Protease I of Escherichia coli functions as a thioesterase in vivo."; RL J. Bacteriol. 176:1793-1795(1994). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE RP SPECIFICITY. RX PubMed=9070299; DOI=10.1006/bbrc.1997.5797; RA Lee Y.L., Chen J.C., Shaw J.F.; RT "The thioesterase I of Escherichia coli has arylesterase activity and shows RT stereospecificity for protease substrates."; RL Biochem. Biophys. Res. Commun. 231:452-456(1997). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY. RX PubMed=10423542; DOI=10.1093/oxfordjournals.jbchem.a022470; RA Karasawa K., Yokoyama K., Setaka M., Nojima S.; RT "The Escherichia coli pldC gene encoding lysophospholipase L(1) is RT identical to the apeA and tesA genes encoding protease I and thioesterase RT I, respectively."; RL J. Biochem. 126:445-448(1999). RN [14] RP ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND RP REACTION MECHANISM. RX PubMed=12846577; DOI=10.1021/bi027246w; RA Tyukhtenko S.I., Litvinchuk A.V., Chang C.F., Lo Y.C., Lee S.J., Shaw J.F., RA Liaw Y.C., Huang T.H.; RT "Sequential structural changes of Escherichia coli thioesterase/protease I RT in the serial formation of Michaelis and tetrahedral complexes with diethyl RT p-nitrophenyl phosphate."; RL Biochemistry 42:8289-8297(2003). RN [15] RP MUTAGENESIS OF SER-36; GLY-70; ASN-99; ASP-180 AND HIS-183, CATALYTIC RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE SITE. RX PubMed=16515533; DOI=10.1042/bj20051645; RA Lee L.-C., Lee Y.-L., Leu R.-J., Shaw J.-F.; RT "Functional role of catalytic triad and oxyanion hole-forming residues on RT enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase RT L1."; RL Biochem. J. 397:69-76(2006). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 27-208 OF WILD-TYPE AND MUTANT RP PRO-135 IN COMPLEX WITH SUBSTRATE ANALOG, ACTIVE SITE, IDENTIFICATION BY RP MASS SPECTROMETRY, AND SUBUNIT. RX PubMed=12842470; DOI=10.1016/s0022-2836(03)00637-5; RA Lo Y.-C., Lin S.-C., Shaw J.-F., Liaw Y.-C.; RT "Crystal structure of Escherichia coli thioesterase I/protease RT I/lysophospholipase L1: consensus sequence blocks constitute the catalytic RT center of SGNH-hydrolases through a conserved hydrogen bond network."; RL J. Mol. Biol. 330:539-551(2003). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 27-208 OF WILD-TYPE AND MUTANT RP PRO-135 IN COMPLEX WITH SUBSTRATE ANALOG, MUTAGENESIS OF LEU-135, AND RP ACTIVE SITE. RX PubMed=15697222; DOI=10.1021/bi048109x; RA Lo Y.-C., Lin S.-C., Shaw J.-F., Liaw Y.-C.; RT "Substrate specificities of Escherichia coli thioesterase I/protease RT I/lysophospholipase L1 are governed by its switch loop movement."; RL Biochemistry 44:1971-1979(2005). CC -!- FUNCTION: TesA is a multifunctional esterase that can act as a CC thioesterase, lysophospholipase and protease (PubMed:8098033, CC PubMed:8432696, PubMed:1864840, PubMed:4945109, PubMed:4554913, CC PubMed:238979, PubMed:791643, PubMed:8132479, PubMed:9070299, CC PubMed:10423542). TesA functions as a thioesterase specific for fatty CC acyl thioesters of greater than ten carbons, with highest activity on CC palmitoyl-CoA, cis-vaccenoyl-CoA and palmitoleoyl-CoA (PubMed:8098033, CC PubMed:4554913, PubMed:8132479, PubMed:9070299, PubMed:10423542). TesA CC also possesses an arylesterase activity towards short acyl-chain CC aromatic esters such as alpha-naphthyl acetate, alpha-naphthyl CC butyrate, benzyl acetate and phenyl acetate (PubMed:9070299). Also able CC to hydrolyze short acyl-chain triacylglycerols such as triacetin and CC tributyrin, and p-nitrophenyl esters such as p-nitrophenyl hexanoate CC and p-nitrophenyl butyrate (PubMed:9070299). The protease activity is CC mainly active on small peptides (PubMed:8432696, PubMed:9070299). TesA CC is also able to hydrolyze p-nitrophenyl esters of N-substituted amino CC acids such as N-benzyloxycarbonyl-L-Phe-p-nitrophenyl ester (Z-L-Phe- CC ONp) and N-benzyloxycarbonyl-L-Tyr-p-nitrophenyl ester (Z-L-Tyr-ONp), CC however it is unable to hydrolyze N-acetyl-L-Phe ethyl ester and its CC Tyr analog (PubMed:8432696, PubMed:791643, PubMed:10423542). TesA also CC hydrolyzes N-benzyloxycarbonyl-L-Phe beta-nitrophenyl ester (Cbz-Phe- CC ONap) and N-acetyl-DL-Phe-2-naphthyl ester (chymotrypsin-like CC specificity) (PubMed:8432696, PubMed:4945109). Shows a slow proteolytic CC activity against denatured casein (PubMed:4945109). The CC lysophospholipase activity of TesA is able to hydrolyze 1-palmitoyl-sn- CC glycero-3-phosphocholine, 1-acyl-sn-glycero-3-phosphoglycerol, 1- and CC 2-acyl-sn-glycero-3-phosphoethanolamine (PubMed:1864840, PubMed:238979, CC PubMed:10423542). {ECO:0000269|PubMed:10423542, CC ECO:0000269|PubMed:1864840, ECO:0000269|PubMed:238979, CC ECO:0000269|PubMed:4554913, ECO:0000269|PubMed:4945109, CC ECO:0000269|PubMed:791643, ECO:0000269|PubMed:8098033, CC ECO:0000269|PubMed:8132479, ECO:0000269|PubMed:8432696, CC ECO:0000269|PubMed:9070299}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); CC Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; CC Evidence={ECO:0000269|PubMed:4554913, ECO:0000269|PubMed:9070299}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16782; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; CC Evidence={ECO:0000269|PubMed:4554913, ECO:0000269|PubMed:9070299}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); CC Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; CC Evidence={ECO:0000269|PubMed:4554913}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; CC Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; CC Evidence={ECO:0000269|PubMed:4554913}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); CC Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; CC Evidence={ECO:0000269|PubMed:4554913}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + CC holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA- CC COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14; CC Evidence={ECO:0000269|PubMed:4554913}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15058; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(11Z)-octadecenoyl-CoA + H2O = (11Z)-octadecenoate + CoA + CC H(+); Xref=Rhea:RHEA:65240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30827, ChEBI:CHEBI:57287, ChEBI:CHEBI:75121; CC Evidence={ECO:0000269|PubMed:4554913}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65241; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; CC Evidence={ECO:0000269|PubMed:4554913}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)- CC eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368; CC Evidence={ECO:0000269|PubMed:4554913}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; CC Evidence={ECO:0000269|PubMed:16515533}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); CC Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; CC Evidence={ECO:0000269|PubMed:4554913}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate; CC Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620; CC Evidence={ECO:0000269|PubMed:4554913}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; CC Evidence={ECO:0000305|PubMed:10423542, ECO:0000305|PubMed:1864840}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); CC Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; CC Evidence={ECO:0000269|PubMed:9070299}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; CC Evidence={ECO:0000269|PubMed:16515533, ECO:0000269|PubMed:9070299}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) + CC hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656; CC Evidence={ECO:0000269|PubMed:9070299}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + CC octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; CC Evidence={ECO:0000269|PubMed:9070299}; CC -!- ACTIVITY REGULATION: Thioesterase activity is inhibited by CC iodoacetamide and photoactivated methylene blue, and slowly inhibited CC by 2,4-dinitrofluorobenzene (PubMed:4554913). Protease and CC lysophospholipase activities are inhibited by CC diisopropylfluorophosphate (DFP) (PubMed:1864840, PubMed:4945109, CC PubMed:238979). Lysophospholipase activity is inhibited by Fe(2+), CC Fe(3+) and Al(3+) ions (PubMed:238979). Diethyl p-nitrophenyl phosphate CC (DENP) irreversibly inhibits both the protease and thioesterase CC activities (PubMed:12846577). {ECO:0000269|PubMed:12846577, CC ECO:0000269|PubMed:1864840, ECO:0000269|PubMed:238979, CC ECO:0000269|PubMed:4554913, ECO:0000269|PubMed:4945109}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.5 uM for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester CC {ECO:0000269|PubMed:9070299}; CC KM=3.8 uM for oleoyl-ACP {ECO:0000269|PubMed:4554913}; CC KM=4 uM for oleoyl-CoA {ECO:0000269|PubMed:4554913}; CC KM=4 uM for palmitoleoyl-CoA {ECO:0000269|PubMed:4554913}; CC KM=4.6 uM for cis-vaccenoyl-CoA {ECO:0000269|PubMed:4554913}; CC KM=6.2 uM for palmitoyl-CoA {ECO:0000269|PubMed:4554913}; CC KM=6.4 uM for myristoyl-CoA {ECO:0000269|PubMed:4554913}; CC KM=7.2 uM for palmitoyl-CoA {ECO:0000269|PubMed:9070299}; CC KM=7.7 uM for stearoyl-CoA {ECO:0000269|PubMed:4554913}; CC KM=9.9 uM for arachidonoyl-CoA {ECO:0000269|PubMed:4554913}; CC KM=11.5 uM for decanoyl-CoA {ECO:0000269|PubMed:4554913}; CC KM=13.2 uM for N-benzyloxycarbonyl-D-tyrosine-p-nitrophenyl ester CC {ECO:0000269|PubMed:9070299}; CC KM=27.3 uM for hexanoyl-CoA {ECO:0000269|PubMed:4554913}; CC KM=110 uM for oleoyl pantetheine {ECO:0000269|PubMed:4554913}; CC KM=146 uM for lauroyl-CoA (at pH 7 and 37 degrees Celsius) CC {ECO:0000269|PubMed:16515533}; CC KM=174 uM for N-carbobenzoxy-L-tyrosine p-nitrophenyl ester (at pH 7 CC and 37 degrees Celsius) {ECO:0000269|PubMed:16515533}; CC KM=200 uM for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester CC {ECO:0000269|PubMed:791643}; CC KM=730 uM for diethyl p-nitrophenyl phosphate CC {ECO:0000269|PubMed:12846577}; CC KM=617.8 uM for p-nitrophenyl decanoate {ECO:0000269|PubMed:9070299}; CC KM=870 uM for p-nitrophenyl butyrate (at pH 7 and 37 degrees Celsius) CC {ECO:0000269|PubMed:16515533}; CC KM=1.46 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:9070299}; CC Vmax=25 umol/min/mg enzyme with CC N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate CC {ECO:0000269|PubMed:791643}; CC Vmax=0.33 umol/min/mg enzyme with diethyl p-nitrophenyl phosphate as CC substrate {ECO:0000269|PubMed:12846577}; CC Vmax=30.1 pmol/min/mg enzyme with palmitoyl-CoA as substrate CC {ECO:0000269|PubMed:4554913}; CC Vmax=20.9 pmol/min/mg enzyme with myristoyl-CoA as substrate CC {ECO:0000269|PubMed:4554913}; CC Vmax=19.7 pmol/min/mg enzyme with stearoyl-CoA as substrate CC {ECO:0000269|PubMed:4554913}; CC Vmax=19.3 pmol/min/mg enzyme with cis-vaccenoyl-CoA as substrate CC {ECO:0000269|PubMed:4554913}; CC Vmax=17 pmol/min/mg enzyme with arachidonoyl-CoA as substrate CC {ECO:0000269|PubMed:4554913}; CC Vmax=15.7 pmol/min/mg enzyme with palmitoleoyl-CoA as substrate CC {ECO:0000269|PubMed:4554913}; CC Vmax=14 pmol/min/mg enzyme with oleoyl-CoA as substrate CC {ECO:0000269|PubMed:4554913}; CC Vmax=9.6 pmol/min/mg enzyme with decanoyl-CoA as substrate CC {ECO:0000269|PubMed:4554913}; CC Vmax=7.7 pmol/min/mg enzyme with hexanoyl-CoA as substrate CC {ECO:0000269|PubMed:4554913}; CC Vmax=7.6 pmol/min/mg enzyme with oleoyl pantetheine as substrate CC {ECO:0000269|PubMed:4554913}; CC Vmax=0.4 pmol/min/mg enzyme with oleoyl-ACP as substrate CC {ECO:0000269|PubMed:4554913}; CC Note=kcat is 88.99 sec(-1) for CC N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate CC (PubMed:16515533). kcat is 62.4 sec(-1) for p-nitrophenyl butyrate as CC substrate (PubMed:9070299). kcat is 15.29 sec(-1) for p-nitrophenyl CC butyrate as substrate (PubMed:16515533). kcat is 14.1 sec(-1) for CC N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate CC (PubMed:9070299). kcat is 10.13 sec(-1) for lauroyl-CoA as substrate CC (PubMed:16515533). kcat is 5.1 sec(-1) for p-nitrophenyl decanoate as CC substrate (PubMed:9070299). kcat is 2.6 sec(-1) for palmitoyl-CoA as CC substrate (PubMed:9070299). kcat is 2.3 sec(-1) for CC N-benzyloxycarbonyl-D-tyrosine-p-nitrophenyl ester as substrate CC (PubMed:9070299). {ECO:0000269|PubMed:16515533, CC ECO:0000269|PubMed:9070299}; CC pH dependence: CC Optimum pH is 7.5-8.4 (PubMed:4945109, PubMed:4554913, CC PubMed:12846577). Stable between pH 6.1 and 12, however, below pH CC 6.0, thioesterase rapidly loses activity (PubMed:4554913). CC {ECO:0000269|PubMed:12846577, ECO:0000269|PubMed:4554913, CC ECO:0000269|PubMed:4945109}; CC Temperature dependence: CC Protease is stable up to 50 degrees Celsius. CC {ECO:0000269|PubMed:4945109}; CC -!- SUBUNIT: Monomer or homotetramer. {ECO:0000269|PubMed:12842470, CC ECO:0000269|PubMed:1864840, ECO:0000269|PubMed:4554913, CC ECO:0000269|PubMed:791643, ECO:0000269|PubMed:8098033}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8098033, CC ECO:0000269|PubMed:8432696}. CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not show thioesterase CC activity and have a little protease activity against Cbz-Phe-ONap. No CC effect on the cell growth and fatty acid composition. CC {ECO:0000269|PubMed:8098033, ECO:0000269|PubMed:8432696}. CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB40248.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L06182; AAA24664.1; -; Genomic_DNA. DR EMBL; D13180; BAA02475.1; -; Genomic_DNA. DR EMBL; U82664; AAB40248.1; ALT_INIT; Genomic_DNA. DR EMBL; U00096; AAC73596.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76273.1; -; Genomic_DNA. DR PIR; A49699; A49699. DR PIR; PX0045; PX0045. DR RefSeq; NP_415027.1; NC_000913.3. DR PDB; 1IVN; X-ray; 1.90 A; A=27-208. DR PDB; 1J00; X-ray; 2.00 A; A=27-208. DR PDB; 1JRL; X-ray; 1.95 A; A=27-208. DR PDB; 1U8U; X-ray; 2.08 A; A=27-208. DR PDB; 1V2G; X-ray; 2.00 A; A=27-208. DR PDB; 5TIC; X-ray; 1.65 A; A/B=28-208. DR PDB; 5TID; X-ray; 1.20 A; A=28-208. DR PDB; 5TIE; X-ray; 1.15 A; A=28-208. DR PDB; 5TIF; X-ray; 0.97 A; A=28-208. DR PDB; 6LFB; X-ray; 1.99 A; A=28-205. DR PDB; 6LFC; X-ray; 2.70 A; A/B/C/D/E/F=28-208. DR PDBsum; 1IVN; -. DR PDBsum; 1J00; -. DR PDBsum; 1JRL; -. DR PDBsum; 1U8U; -. DR PDBsum; 1V2G; -. DR PDBsum; 5TIC; -. DR PDBsum; 5TID; -. DR PDBsum; 5TIE; -. DR PDBsum; 5TIF; -. DR PDBsum; 6LFB; -. DR PDBsum; 6LFC; -. DR AlphaFoldDB; P0ADA1; -. DR BMRB; P0ADA1; -. DR SMR; P0ADA1; -. DR BioGRID; 4259854; 5. DR STRING; 511145.b0494; -. DR DrugBank; DB02364; 2-Amino-3-(Diethoxy-Phosphoryloxy)-Propionic Acid. DR DrugBank; DB04519; Caprylic acid. DR DrugBank; DB03366; Imidazole. DR SwissLipids; SLP:000001818; -. DR MEROPS; X42.001; -. DR jPOST; P0ADA1; -. DR PaxDb; 511145-b0494; -. DR EnsemblBacteria; AAC73596; AAC73596; b0494. DR GeneID; 945127; -. DR KEGG; ecj:JW0483; -. DR KEGG; eco:b0494; -. DR PATRIC; fig|511145.12.peg.515; -. DR EchoBASE; EB1504; -. DR eggNOG; COG2755; Bacteria. DR HOGENOM; CLU_051180_3_0_6; -. DR InParanoid; P0ADA1; -. DR OMA; MRIPPNY; -. DR PhylomeDB; P0ADA1; -. DR BioCyc; EcoCyc:THIOESTERI-MONOMER; -. DR BioCyc; MetaCyc:THIOESTERI-MONOMER; -. DR BRENDA; 3.1.1.5; 2026. DR BRENDA; 3.1.2.2; 2026. DR SABIO-RK; P0ADA1; -. DR EvolutionaryTrace; P0ADA1; -. DR PRO; PR:P0ADA1; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc. DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:EcoCyc. DR GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0004622; F:lysophospholipase activity; IDA:EcoCyc. DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:RHEA. DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:EcoCyc. DR GO; GO:0008233; F:peptidase activity; IDA:EcoCyc. DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC. DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd01822; Lysophospholipase_L1_like; 1. DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1. DR InterPro; IPR008265; Lipase_GDSL_AS. DR InterPro; IPR013830; SGNH_hydro. DR InterPro; IPR036514; SGNH_hydro_sf. DR PANTHER; PTHR30383; THIOESTERASE 1/PROTEASE 1/LYSOPHOSPHOLIPASE L1; 1. DR PANTHER; PTHR30383:SF5; THIOESTERASE 1_PROTEASE 1_LYSOPHOSPHOLIPASE L1; 1. DR Pfam; PF13472; Lipase_GDSL_2; 1. DR SUPFAM; SSF52266; SGNH hydrolase; 1. DR PROSITE; PS01098; LIPASE_GDSL_SER; 1. DR SWISS-2DPAGE; P0ADA1; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Hydrolase; Lipid metabolism; KW Periplasm; Protease; Reference proteome; Signal. FT SIGNAL 1..26 FT /evidence="ECO:0000269|PubMed:1864840, FT ECO:0000269|PubMed:8098033, ECO:0000269|PubMed:8432696" FT CHAIN 27..208 FT /note="Thioesterase 1/protease 1/lysophospholipase L1" FT /id="PRO_0000017848" FT ACT_SITE 36 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:15697222, FT ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, FT ECO:0000305|PubMed:12846577, ECO:0000305|PubMed:8098033" FT ACT_SITE 180 FT /evidence="ECO:0000269|PubMed:15697222, FT ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, FT ECO:0000305|PubMed:12846577" FT ACT_SITE 183 FT /evidence="ECO:0000269|PubMed:15697222, FT ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, FT ECO:0000305|PubMed:12846577" FT BINDING 70 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15697222" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15697222" FT MUTAGEN 36 FT /note="S->A: Loss of hydrolysis activity." FT /evidence="ECO:0000269|PubMed:16515533" FT MUTAGEN 70 FT /note="G->A: Retains weak hydrolysis activity." FT /evidence="ECO:0000269|PubMed:16515533" FT MUTAGEN 99 FT /note="N->A: Retains weak hydrolysis activity." FT /evidence="ECO:0000269|PubMed:16515533" FT MUTAGEN 135 FT /note="L->P: Abolishes switch loop movement. Lowers FT activity towards substrates with long acyl chains." FT /evidence="ECO:0000269|PubMed:15697222" FT MUTAGEN 180 FT /note="D->A: Retains weak hydrolysis activity." FT /evidence="ECO:0000269|PubMed:16515533" FT MUTAGEN 183 FT /note="H->A: Loss of hydrolysis activity." FT /evidence="ECO:0000269|PubMed:16515533" FT STRAND 28..35 FT /evidence="ECO:0007829|PDB:5TIF" FT HELIX 36..39 FT /evidence="ECO:0007829|PDB:5TIF" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:1IVN" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:5TIF" FT HELIX 49..57 FT /evidence="ECO:0007829|PDB:5TIF" FT STRAND 60..67 FT /evidence="ECO:0007829|PDB:5TIF" FT HELIX 73..87 FT /evidence="ECO:0007829|PDB:5TIF" FT STRAND 90..95 FT /evidence="ECO:0007829|PDB:5TIF" FT HELIX 98..102 FT /evidence="ECO:0007829|PDB:5TIF" FT HELIX 107..123 FT /evidence="ECO:0007829|PDB:5TIF" FT STRAND 127..131 FT /evidence="ECO:0007829|PDB:5TIF" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:1IVN" FT HELIX 141..158 FT /evidence="ECO:0007829|PDB:5TIF" FT HELIX 167..171 FT /evidence="ECO:0007829|PDB:5TIF" FT HELIX 174..176 FT /evidence="ECO:0007829|PDB:5TIF" FT STRAND 181..184 FT /evidence="ECO:0007829|PDB:5TIF" FT HELIX 188..204 FT /evidence="ECO:0007829|PDB:5TIF" SQ SEQUENCE 208 AA; 23622 MW; CD03F23EA39541F1 CRC64; MMNFNNVFRW HLPFLFLVLL TFRAAAADTL LILGDSLSAG YRMSASAAWP ALLNDKWQSK TSVVNASISG DTSQQGLARL PALLKQHQPR WVLVELGGND GLRGFQPQQT EQTLRQILQD VKAANAEPLL MQIRLPANYG RRYNEAFSAI YPKLAKEFDV PLLPFFMEEV YLKPQWMQDD GIHPNRDAQP FIADWMAKQL QPLVNHDS //