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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei36 – 361NucleophileBy similarity
Binding sitei70 – 701Substrate; via amide nitrogen
Binding sitei99 – 991Substrate
Active sitei180 – 1801By similarity
Active sitei183 – 18311 Publication

GO - Molecular functioni

  1. acyl-CoA hydrolase activity Source: EcoCyc
  2. identical protein binding Source: EcoCyc
  3. lysophospholipase activity Source: EcoCyc
  4. palmitoyl-CoA hydrolase activity Source: EcoCyc
  5. peptidase activity Source: EcoCyc
  6. phospholipase activity Source: EcoCyc

GO - Biological processi

  1. lipid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

BioCyciEcoCyc:THIOESTERI-MONOMER.
ECOL316407:JW0483-MONOMER.
MetaCyc:THIOESTERI-MONOMER.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11542. tesA.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361S → A: Reduces activity by over 99%. 1 Publication
Mutagenesisi70 – 701G → A: Reduces activity by over 75%. 1 Publication
Mutagenesisi99 – 991N → A: Reduces activity by over 60%. 1 Publication
Mutagenesisi135 – 1351L → P: Lowers activity towards substrates with long acyl chains.
Mutagenesisi180 – 1801D → A: Reduces activity by over 70%. 1 Publication
Mutagenesisi183 – 1831H → A: Reduces activity by over 99%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26262 PublicationsAdd
BLAST
Chaini27 – 208182Acyl-CoA thioesterase IPRO_0000017848Add
BLAST

Proteomic databases

PaxDbiP0ADA1.
PRIDEiP0ADA1.

2D gel databases

SWISS-2DPAGEP0ADA1.

Expressioni

Gene expression databases

GenevestigatoriP0ADA1.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi511145.b0494.

Structurei

Secondary structure

1
208
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 347Combined sources
Helixi36 – 394Combined sources
Beta strandi41 – 433Combined sources
Helixi45 – 473Combined sources
Helixi49 – 568Combined sources
Turni57 – 604Combined sources
Beta strandi61 – 655Combined sources
Helixi73 – 8715Combined sources
Beta strandi90 – 956Combined sources
Turni98 – 1014Combined sources
Beta strandi102 – 1043Combined sources
Helixi107 – 12317Combined sources
Beta strandi127 – 1315Combined sources
Helixi137 – 1393Combined sources
Helixi141 – 15717Combined sources
Helixi167 – 1715Combined sources
Helixi174 – 1763Combined sources
Beta strandi181 – 1844Combined sources
Helixi186 – 1883Combined sources
Helixi189 – 20012Combined sources
Turni201 – 2044Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 27-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADA1.

Family & Domainsi

Sequence similaritiesi

Belongs to the 'GDSL' lipolytic enzyme family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2755.
HOGENOMiHOG000261382.
InParanoidiP0ADA1.
KOiK10804.
OMAiRGFPPQQ.
OrthoDBiEOG6PGK4B.
PhylomeDBiP0ADA1.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR001087. Lipase_GDSL.
IPR008265. Lipase_GDSL_AS.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
PfamiPF00657. Lipase_GDSL. 1 hit.
[Graphical view]
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 AAB40248.1 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.
YP_488785.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73596; AAC73596; b0494.
BAE76273; BAE76273; BAE76273.
GeneIDi12930860.
945127.
KEGGiecj:Y75_p0481.
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.
YP_488785.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 27-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi511145.b0494.

2D gel databases

SWISS-2DPAGEP0ADA1.

Proteomic databases

PaxDbiP0ADA1.
PRIDEiP0ADA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73596; AAC73596; b0494.
BAE76273; BAE76273; BAE76273.
GeneIDi12930860.
945127.
KEGGiecj:Y75_p0481.
eco:b0494.
PATRICi32116147. VBIEscCol129921_0515.

Organism-specific databases

EchoBASEiEB1504.
EcoGeneiEG11542. tesA.

Phylogenomic databases

eggNOGiCOG2755.
HOGENOMiHOG000261382.
InParanoidiP0ADA1.
KOiK10804.
OMAiRGFPPQQ.
OrthoDBiEOG6PGK4B.
PhylomeDBiP0ADA1.

Enzyme and pathway databases

BioCyciEcoCyc:THIOESTERI-MONOMER.
ECOL316407:JW0483-MONOMER.
MetaCyc:THIOESTERI-MONOMER.
SABIO-RKP0ADA1.

Miscellaneous databases

EvolutionaryTraceiP0ADA1.
PROiP0ADA1.

Gene expression databases

GenevestigatoriP0ADA1.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR001087. Lipase_GDSL.
IPR008265. Lipase_GDSL_AS.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
PfamiPF00657. Lipase_GDSL. 1 hit.
[Graphical view]
PROSITEiPS01098. LIPASE_GDSL_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme."
    Cho H., Cronan J.E. Jr.
    J. Biol. Chem. 268:9238-9245(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of proteinase and proteinase-defective Escherichia coli mutants."
    Ichihara S., Matsubara Y., Kato C., Akasaka K., Mizushima S.
    J. Bacteriol. 175:1032-1037(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-38.
    Strain: K12.
  3. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Lysophospholipase L1 from Escherichia coli K-12 overproducer."
    Karasawa K., Kudo I., Kobayashi T., Homma H., Chiba N., Mizushima H., Inoue K., Nojima S.
    J. Biochem. 109:288-293(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-43, CHARACTERIZATION AS LYSOPHOSPHOLIPASE.
    Strain: K12.
  7. "Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1."
    Lee L.-C., Lee Y.-L., Leu R.-J., Shaw J.-F.
    Biochem. J. 397:69-76(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-36; GLY-70; ASN-99; ASP-180 AND HIS-183.
  8. "Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network."
    Lo Y.-C., Lin S.-C., Shaw J.-F., Liaw Y.-C.
    J. Mol. Biol. 330:539-551(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 27-208 IN COMPLEX WITH SUBSTRATE ANALOG, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement."
    Lo Y.-C., Lin S.-C., Shaw J.-F., Liaw Y.-C.
    Biochemistry 44:1971-1979(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 27-208 OF WILD-TYPE AND MUTANT PRO-135 IN COMPLEX WITH SUBSTRATE ANALOG.

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: January 7, 2015
This is version 79 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

External Data

Dasty 3

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 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.