TESA_ECOLI
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 03-AUG-2022, entry version 125.
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},
GN pldC {ECO:0000303|PubMed:1864840}; OrderedLocusNames=b0494, JW0483;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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 N-benzyloxycarbonyl-L-tyrosine-p-
CC nitrophenyl ester as substrate {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 N-benzyloxycarbonyl-L-tyrosine-p-
CC nitrophenyl ester as substrate (PubMed:16515533). kcat is 62.4 sec(-
CC 1) for p-nitrophenyl butyrate as substrate (PubMed:9070299). kcat is
CC 15.29 sec(-1) for p-nitrophenyl butyrate as substrate
CC (PubMed:16515533). kcat is 14.1 sec(-1) for N-benzyloxycarbonyl-L-
CC tyrosine-p-nitrophenyl ester as substrate (PubMed:9070299). kcat is
CC 10.13 sec(-1) for lauroyl-CoA as substrate (PubMed:16515533). kcat is
CC 5.1 sec(-1) for p-nitrophenyl decanoate as substrate
CC (PubMed:9070299). kcat is 2.6 sec(-1) for palmitoyl-CoA as substrate
CC (PubMed:9070299). kcat is 2.3 sec(-1) for N-benzyloxycarbonyl-D-
CC tyrosine-p-nitrophenyl ester as substrate (PubMed:9070299).
CC {ECO:0000269|PubMed:16515533, 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};
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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 SWISS-2DPAGE; P0ADA1; -.
DR jPOST; P0ADA1; -.
DR PaxDb; P0ADA1; -.
DR PRIDE; P0ADA1; -.
DR EnsemblBacteria; AAC73596; AAC73596; b0494.
DR EnsemblBacteria; BAE76273; BAE76273; BAE76273.
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-MON; -.
DR BioCyc; MetaCyc:THIOESTERI-MON; -.
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:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR008265; Lipase_GDSL_AS.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
DR PROSITE; PS01098; LIPASE_GDSL_SER; 1.
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
