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Protein

Acyl-CoA thioesterase I

Gene

tesA

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

Functioni

Hydrolyzes only long chain acyl thioesters (C12-C18). Specificity similar to chymotrypsin.

Catalytic activityi

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei36NucleophileBy similarity1
Binding sitei70Substrate; via amide nitrogen1
Binding sitei99Substrate1
Active sitei180By similarity1
Active sitei1831 Publication1

GO - Molecular functioni

  • acyl-CoA hydrolase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • lysophospholipase activity Source: EcoCyc
  • palmitoyl-CoA hydrolase activity Source: EcoCyc
  • peptidase activity Source: EcoCyc
  • phospholipase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

BioCyciEcoCyc:THIOESTERI-MONOMER.
ECOL316407:JW0483-MONOMER.
MetaCyc:THIOESTERI-MONOMER.
BRENDAi3.1.1.5. 2026.
3.1.2.2. 2026.
SABIO-RKP0ADA1.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA thioesterase I (EC:3.1.2.-)
Alternative name(s):
Lecithinase B
Lysophospholipase L1 (EC:3.1.1.5)
Protease I
Gene namesi
Name:tesA
Synonyms:apeA, pldC
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

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi36S → A: Reduces activity by over 99%. 1 Publication1
Mutagenesisi70G → A: Reduces activity by over 75%. 1 Publication1
Mutagenesisi99N → A: Reduces activity by over 60%. 1 Publication1
Mutagenesisi135L → P: Lowers activity towards substrates with long acyl chains. 1
Mutagenesisi180D → A: Reduces activity by over 70%. 1 Publication1
Mutagenesisi183H → A: Reduces activity by over 99%. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 262 PublicationsAdd BLAST26
ChainiPRO_000001784827 – 208Acyl-CoA thioesterase IAdd BLAST182

Proteomic databases

EPDiP0ADA1.
PaxDbiP0ADA1.
PRIDEiP0ADA1.

2D gel databases

SWISS-2DPAGEP0ADA1.

Interactioni

Subunit structurei

Monomer.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259854. 5 interactors.
STRINGi511145.b0494.

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[»]
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.
OMAiPPNYGPD.
PhylomeDBiP0ADA1.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR008265. Lipase_GDSL_AS.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF13472. Lipase_GDSL_2. 1 hit.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 1 hit.
PROSITEiPS01098. LIPASE_GDSL_SER. 1 hit.
[Graphical view]

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.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.

Genome annotation databases

EnsemblBacteriaiAAC73596; AAC73596; b0494.
BAE76273; BAE76273; BAE76273.
GeneIDi945127.
KEGGiecj:JW0483.
eco:b0494.
PATRICi32116147. VBIEscCol129921_0515.

Cross-referencesi

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.

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[»]
ProteinModelPortaliP0ADA1.
SMRiP0ADA1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259854. 5 interactors.
STRINGi511145.b0494.

2D gel databases

SWISS-2DPAGEP0ADA1.

Proteomic databases

EPDiP0ADA1.
PaxDbiP0ADA1.
PRIDEiP0ADA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73596; AAC73596; b0494.
BAE76273; BAE76273; BAE76273.
GeneIDi945127.
KEGGiecj:JW0483.
eco:b0494.
PATRICi32116147. VBIEscCol129921_0515.

Organism-specific databases

EchoBASEiEB1504.
EcoGeneiEG11542. tesA.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciEcoCyc:THIOESTERI-MONOMER.
ECOL316407:JW0483-MONOMER.
MetaCyc:THIOESTERI-MONOMER.
BRENDAi3.1.1.5. 2026.
3.1.2.2. 2026.
SABIO-RKP0ADA1.

Miscellaneous databases

EvolutionaryTraceiP0ADA1.
PROiP0ADA1.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR008265. Lipase_GDSL_AS.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF13472. Lipase_GDSL_2. 1 hit.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 1 hit.
PROSITEiPS01098. LIPASE_GDSL_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTESA_ECOLI
AccessioniPrimary (citable) accession number: P0ADA1
Secondary accession number(s): P29679
, P37331, P77125, Q2MBT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: November 2, 2016
This is version 91 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.