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Protein

Thioesterase 1/protease 1/lysophospholipase L1

Gene

tesA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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-vaccenyl-CoA and palmitoleyl-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).10 Publications

Catalytic activityi

Palmitoyl-CoA + H2O = CoA + palmitate.1 Publication
2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.2 Publications
A phenyl acetate + H2O = a phenol + acetate.1 Publication
Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.1 Publication

Enzyme regulationi

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 Fe2+, Fe3+ and Al3+ ions (PubMed:238979). Diethyl p-nitrophenyl phosphate (DENP) irreversibly inhibits both the protease and thioesterase activities (PubMed:12846577).5 Publications

Kineticsi

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 decaonate 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).2 Publications
  1. KM=3.5 µM for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester1 Publication
  2. KM=3.8 µM for oleyl-ACP1 Publication
  3. KM=4 µM for oleyl-CoA1 Publication
  4. KM=4 µM for palmitoleyl-CoA1 Publication
  5. KM=4.6 µM for cis-vaccenoyl-CoA1 Publication
  6. KM=6.2 µM for palmitoyl-CoA1 Publication
  7. KM=6.4 µM for myristoyl-CoA1 Publication
  8. KM=7.2 µM for palmitoyl-CoA1 Publication
  9. KM=7.7 µM for stearoyl-CoA1 Publication
  10. KM=9.9 µM for arachidoyl-CoA1 Publication
  11. KM=11.5 µM for decanoyl-CoA1 Publication
  12. KM=13.2 µM for N-benzyloxycarbonyl-D-tyrosine-p-nitrophenyl ester1 Publication
  13. KM=27.3 µM for hexanoyl-CoA1 Publication
  14. KM=110 µM for oleyl pantetheine1 Publication
  15. KM=146 µM for lauroyl-CoA (at pH 7 and 37 degrees Celsius)1 Publication
  16. KM=174 µM for N-carbobenzoxy-L-tyrosine p-nitrophenyl ester (at pH 7 and 37 degrees Celsius)1 Publication
  17. KM=200 µM for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester1 Publication
  18. KM=730 µM for diethyl p-nitrophenyl phosphate1 Publication
  19. KM=617.8 µM for p-nitrophenyl decaonate1 Publication
  20. KM=870 µM for p-nitrophenyl butyrate (at pH 7 and 37 degrees Celsius)1 Publication
  21. KM=1.46 mM for p-nitrophenyl butyrate1 Publication
  1. Vmax=25 µmol/min/mg enzyme with N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate1 Publication
  2. Vmax=0.33 µmol/min/mg enzyme with diethyl p-nitrophenyl phosphate as substrate1 Publication
  3. Vmax=30.1 pmol/min/mg enzyme with palmitoyl-CoA as substrate1 Publication
  4. Vmax=20.9 pmol/min/mg enzyme with myristoyl-CoA as substrate1 Publication
  5. Vmax=19.7 pmol/min/mg enzyme with stearoyl-CoA as substrate1 Publication
  6. Vmax=19.3 pmol/min/mg enzyme with cis-vaccenoyl-CoA as substrate1 Publication
  7. Vmax=17 pmol/min/mg enzyme with arachidoyl-CoA as substrate1 Publication
  8. Vmax=15.7 pmol/min/mg enzyme with palmitoleyl-CoA as substrate1 Publication
  9. Vmax=14 pmol/min/mg enzyme with oleyl-CoA as substrate1 Publication
  10. Vmax=9.6 pmol/min/mg enzyme with decanoyl-CoA as substrate1 Publication
  11. Vmax=7.7 pmol/min/mg enzyme with hexanoyl-CoA as substrate1 Publication
  12. Vmax=7.6 pmol/min/mg enzyme with oleyl pantetheine as substrate1 Publication
  13. Vmax=0.4 pmol/min/mg enzyme with oleyl-ACP as substrate1 Publication

pH dependencei

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).3 Publications

Temperature dependencei

Protease is stable up to 50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei36Nucleophile3 Publications2 Publications1
Binding sitei70Substrate; via amide nitrogen1 Publication1
Binding sitei99Substrate1 Publication1
Active sitei1802 Publications2 Publications1
Active sitei1832 Publications2 Publications1

GO - Molecular functioni

  • acyl-CoA hydrolase activity Source: EcoCyc
  • arylesterase activity Source: UniProtKB-EC
  • identical protein binding Source: EcoCyc
  • lysophospholipase activity Source: EcoCyc
  • myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  • myristoyl-CoA hydrolase activity Source: UniProtKB-EC
  • oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  • palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  • palmitoyl-CoA hydrolase activity Source: EcoCyc
  • peptidase activity Source: EcoCyc
  • phospholipase activity Source: EcoCyc

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease

Enzyme and pathway databases

BioCyciEcoCyc:THIOESTERI-MONOMER.
MetaCyc:THIOESTERI-MONOMER.
BRENDAi3.1.1.5. 2026.
3.1.2.2. 2026.
SABIO-RKiP0ADA1.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioesterase 1/protease 1/lysophospholipase L11 Publication
Short name:
TAP1 Publication
Alternative name(s):
Acyl-CoA thioesterase 11 Publication (EC:3.1.2.21 Publication)
Short name:
TESA1 Publication
Acyl-CoA thioesterase I1 Publication
Arylesterase1 Publication (EC:3.1.1.21 Publication)
Lysophospholipase L11 Publication (EC:3.1.1.52 Publications)
Oleoyl-[acyl-carrier-protein] hydrolase1 Publication (EC:3.1.2.141 Publication)
Phospholipid degradation C1 Publication
Short name:
Pldc1 Publication
Protease 11 Publication (EC:3.4.21.-1 Publication)
Protease I1 Publication
Thioesterase I/protease I1 Publication
Short name:
TEP-I1 Publication
Gene namesi
Name:tesA1 Publication
Synonyms:apeA1 Publication, pldC1 Publication
Ordered Locus Names:b0494, JW0483
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11542. tesA.

Subcellular locationi

  • Periplasm 2 Publications

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi36S → A: Loss of hydrolysis activity. 1 Publication1
Mutagenesisi70G → A: Retains weak hydrolysis activity. 1 Publication1
Mutagenesisi99N → A: Retains weak hydrolysis activity. 1 Publication1
Mutagenesisi135L → P: Abolishes switch loop movement. Lowers activity towards substrates with long acyl chains. 1 Publication1
Mutagenesisi180D → A: Retains weak hydrolysis activity. 1 Publication1
Mutagenesisi183H → A: Loss of hydrolysis activity. 1 Publication1

Chemistry databases

DrugBankiDB02364. 2-Amino-3-(Diethoxy-Phosphoryloxy)-Propionic Acid.
DB04519. Caprylic acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 263 PublicationsAdd BLAST26
ChainiPRO_000001784827 – 208Thioesterase 1/protease 1/lysophospholipase L1Add BLAST182

Proteomic databases

PaxDbiP0ADA1.
PRIDEiP0ADA1.

2D gel databases

SWISS-2DPAGEiP0ADA1.

Interactioni

Subunit structurei

Monomer or homotetramer.5 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259854. 5 interactors.
STRINGi316385.ECDH10B_0451.

Structurei

Secondary structure

1208
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 34Combined sources7
Helixi36 – 39Combined sources4
Beta strandi41 – 43Combined sources3
Helixi45 – 47Combined sources3
Helixi49 – 56Combined sources8
Turni57 – 60Combined sources4
Beta strandi61 – 65Combined sources5
Helixi73 – 87Combined sources15
Beta strandi90 – 95Combined sources6
Turni98 – 101Combined sources4
Beta strandi102 – 104Combined sources3
Helixi107 – 123Combined sources17
Beta strandi127 – 131Combined sources5
Helixi137 – 139Combined sources3
Helixi141 – 157Combined sources17
Helixi167 – 171Combined sources5
Helixi174 – 176Combined sources3
Beta strandi181 – 184Combined sources4
Helixi186 – 188Combined sources3
Helixi189 – 200Combined sources12
Turni201 – 204Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IVNX-ray1.90A27-208[»]
1J00X-ray2.00A27-208[»]
1JRLX-ray1.95A27-208[»]
1U8UX-ray2.08A27-208[»]
1V2GX-ray2.00A27-208[»]
5TICX-ray1.65A/B28-208[»]
5TIDX-ray1.20A28-208[»]
5TIEX-ray1.15A28-208[»]
5TIFX-ray0.97A28-208[»]
ProteinModelPortaliP0ADA1.
SMRiP0ADA1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADA1.

Family & Domainsi

Sequence similaritiesi

Belongs to the 'GDSL' lipolytic enzyme family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108UJV. Bacteria.
COG2755. LUCA.
HOGENOMiHOG000261382.
InParanoidiP0ADA1.
KOiK10804.
PhylomeDBiP0ADA1.

Family and domain databases

InterProiView protein in InterPro
IPR008265. Lipase_GDSL_AS.
IPR013830. SGNH_hydro.
PfamiView protein in Pfam
PF13472. Lipase_GDSL_2. 1 hit.
SUPFAMiSSF52266. SSF52266. 1 hit.
PROSITEiView protein in PROSITE
PS01098. LIPASE_GDSL_SER. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ADA1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMNFNNVFRW HLPFLFLVLL TFRAAAADTL LILGDSLSAG YRMSASAAWP
60 70 80 90 100
ALLNDKWQSK TSVVNASISG DTSQQGLARL PALLKQHQPR WVLVELGGND
110 120 130 140 150
GLRGFQPQQT EQTLRQILQD VKAANAEPLL MQIRLPANYG RRYNEAFSAI
160 170 180 190 200
YPKLAKEFDV PLLPFFMEEV YLKPQWMQDD GIHPNRDAQP FIADWMAKQL

QPLVNHDS
Length:208
Mass (Da):23,622
Last modified:December 6, 2005 - v1
Checksum:iCD03F23EA39541F1
GO

Sequence cautioni

The sequence AAB40248 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06182 Genomic DNA. Translation: AAA24664.1.
D13180 Genomic DNA. Translation: BAA02475.1.
U82664 Genomic DNA. Translation: AAB40248.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73596.1.
AP009048 Genomic DNA. Translation: BAE76273.1.
PIRiA49699.
PX0045.
RefSeqiNP_415027.1. NC_000913.3.
WP_001297298.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73596; AAC73596; b0494.
BAE76273; BAE76273; BAE76273.
GeneIDi945127.
KEGGiecj:JW0483.
eco:b0494.
PATRICifig|511145.12.peg.515.

Similar proteinsi

Entry informationi

Entry nameiTESA_ECOLI
AccessioniPrimary (citable) accession number: P0ADA1
Secondary accession number(s): P29679
, P37331, P77125, Q2MBT3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: August 30, 2017
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families