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Thioesterase 1/protease 1/lysophospholipase L1 (TAP) (Acyl-CoA thioesterase 1) (TESA) (EC 3.1.2.2) (Acyl-CoA thioesterase I) (Arylesterase) (EC 3.1.1.2) (Lysophospholipase L1) (EC 3.1.1.5) (Oleoyl-[acyl-carrier-protein] hydrolase) (EC 3.1.2.14) (Phospholipid degradation C) (Pldc) (Protease 1) (EC 3.4.21.-) (Protease I) (Thioesterase I/protease I) (TEP-I)

 TESA_ECOL6              Reviewed;         208 AA.
P0ADA2; P29679; P37331; P77125;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
28-MAR-2018, entry version 74.
RecName: Full=Thioesterase 1/protease 1/lysophospholipase L1 {ECO:0000250|UniProtKB:P0ADA1};
Short=TAP {ECO:0000250|UniProtKB:P0ADA1};
AltName: Full=Acyl-CoA thioesterase 1 {ECO:0000250|UniProtKB:P0ADA1};
Short=TESA {ECO:0000250|UniProtKB:P0ADA1};
EC=3.1.2.2 {ECO:0000250|UniProtKB:P0ADA1};
AltName: Full=Acyl-CoA thioesterase I {ECO:0000250|UniProtKB:P0ADA1};
AltName: Full=Arylesterase {ECO:0000250|UniProtKB:P0ADA1};
EC=3.1.1.2 {ECO:0000250|UniProtKB:P0ADA1};
AltName: Full=Lysophospholipase L1 {ECO:0000250|UniProtKB:P0ADA1};
EC=3.1.1.5 {ECO:0000250|UniProtKB:P0ADA1};
AltName: Full=Oleoyl-[acyl-carrier-protein] hydrolase {ECO:0000250|UniProtKB:P0ADA1};
EC=3.1.2.14 {ECO:0000250|UniProtKB:P0ADA1};
AltName: Full=Phospholipid degradation C {ECO:0000250|UniProtKB:P0ADA1};
Short=Pldc {ECO:0000250|UniProtKB:P0ADA1};
AltName: Full=Protease 1 {ECO:0000250|UniProtKB:P0ADA1};
EC=3.4.21.- {ECO:0000250|UniProtKB:P0ADA1};
AltName: Full=Protease I {ECO:0000250|UniProtKB:P0ADA1};
AltName: Full=Thioesterase I/protease I {ECO:0000250|UniProtKB:P0ADA1};
Short=TEP-I {ECO:0000250|UniProtKB:P0ADA1};
Flags: Precursor;
Name=tesA; OrderedLocusNames=c0615;
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=199310;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CFT073 / ATCC 700928 / UPEC;
PubMed=12471157; DOI=10.1073/pnas.252529799;
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence
of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
-!- FUNCTION: TesA is a multifunctional esterase that can act as a
thioesterase, arylesterase, lysophospholipase and protease.
{ECO:0000250|UniProtKB:P0ADA1}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + H(2)O = CoA + palmitate.
{ECO:0000250|UniProtKB:P0ADA1}.
-!- CATALYTIC ACTIVITY: 2-lysophosphatidylcholine + H(2)O =
glycerophosphocholine + a carboxylate.
{ECO:0000250|UniProtKB:P0ADA1}.
-!- CATALYTIC ACTIVITY: A phenyl acetate + H(2)O = a phenol + acetate.
{ECO:0000250|UniProtKB:P0ADA1}.
-!- CATALYTIC ACTIVITY: Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-
carrier-protein] + oleate. {ECO:0000250|UniProtKB:P0ADA1}.
-!- SUBUNIT: Monomer or homotetramer. {ECO:0000250|UniProtKB:P0ADA1}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P0ADA1}.
-!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAN79092.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AE014075; AAN79092.1; ALT_INIT; Genomic_DNA.
RefSeq; WP_001297298.1; NC_004431.1.
ProteinModelPortal; P0ADA2; -.
SMR; P0ADA2; -.
STRING; 199310.c0615; -.
EnsemblBacteria; AAN79092; AAN79092; c0615.
KEGG; ecc:c0615; -.
eggNOG; ENOG4108UJV; Bacteria.
eggNOG; COG2755; LUCA.
HOGENOM; HOG000261382; -.
KO; K10804; -.
OMA; TAGYGLP; -.
Proteomes; UP000001410; Chromosome.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-EC.
GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
Gene3D; 3.40.50.1110; -; 1.
InterPro; IPR008265; Lipase_GDSL_AS.
InterPro; IPR013830; SGNH_hydro.
InterPro; IPR036514; SGNH_hydro_sf.
Pfam; PF13472; Lipase_GDSL_2; 1.
PROSITE; PS01098; LIPASE_GDSL_SER; 1.
3: Inferred from homology;
Complete proteome; Hydrolase; Periplasm; Protease; Signal.
SIGNAL 1 26 {ECO:0000250|UniProtKB:P0ADA1}.
CHAIN 27 208 Thioesterase 1/protease
1/lysophospholipase L1.
/FTId=PRO_0000043365.
ACT_SITE 36 36 Nucleophile.
{ECO:0000250|UniProtKB:P0ADA1}.
ACT_SITE 180 180 {ECO:0000250|UniProtKB:P0ADA1}.
ACT_SITE 183 183 {ECO:0000250|UniProtKB:P0ADA1}.
BINDING 70 70 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:P0ADA1}.
BINDING 99 99 Substrate.
{ECO:0000250|UniProtKB:P0ADA1}.
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


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