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P0ADA1 (TESA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-CoA thioesterase I

EC=3.1.2.-
Alternative name(s):
Lecithinase B
Lysophospholipase L1
EC=3.1.1.5
Protease I
Gene names
Name:tesA
Synonyms:apeA, pldC
Ordered Locus Names:b0494, JW0483
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Subunit structure

Monomer.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the 'GDSL' lipolytic enzyme family.

Sequence caution

The sequence AAB40248.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.2 Ref.6
Chain27 – 208182Acyl-CoA thioesterase I
PRO_0000017848

Sites

Active site361Nucleophile By similarity
Active site1801 By similarity
Active site1831 Ref.8
Binding site701Substrate; via amide nitrogen
Binding site991Substrate

Experimental info

Mutagenesis361S → A: Reduces activity by over 99%. Ref.7
Mutagenesis701G → A: Reduces activity by over 75%. Ref.7
Mutagenesis991N → A: Reduces activity by over 60%. Ref.7
Mutagenesis1351L → P: Lowers activity towards substrates with long acyl chains.
Mutagenesis1801D → A: Reduces activity by over 70%. Ref.7
Mutagenesis1831H → A: Reduces activity by over 99%. Ref.7

Secondary structure

...................................... 208
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ADA1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: CD03F23EA39541F1

FASTA20823,622
        10         20         30         40         50         60 
MMNFNNVFRW HLPFLFLVLL TFRAAAADTL LILGDSLSAG YRMSASAAWP ALLNDKWQSK 

        70         80         90        100        110        120 
TSVVNASISG DTSQQGLARL PALLKQHQPR WVLVELGGND GLRGFQPQQT EQTLRQILQD 

       130        140        150        160        170        180 
VKAANAEPLL MQIRLPANYG RRYNEAFSAI YPKLAKEFDV PLLPFFMEEV YLKPQWMQDD 

       190        200 
GIHPNRDAQP FIADWMAKQL QPLVNHDS 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA49699.
PX0045.
RefSeqNP_415027.1. NC_000913.3.
YP_488785.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IVNX-ray1.90A27-208[»]
1J00X-ray2.00A27-208[»]
1JRLX-ray1.95A27-208[»]
1U8UX-ray2.08A27-208[»]
1V2GX-ray2.00A27-208[»]
ProteinModelPortalP0ADA1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b0494.

2D gel databases

SWISS-2DPAGEP0ADA1.

Proteomic databases

PaxDbP0ADA1.
PRIDEP0ADA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73596; AAC73596; b0494.
BAE76273; BAE76273; BAE76273.
GeneID12930860.
945127.
KEGGecj:Y75_p0481.
eco:b0494.
PATRIC32116147. VBIEscCol129921_0515.

Organism-specific databases

EchoBASEEB1504.
EcoGeneEG11542. tesA.

Phylogenomic databases

eggNOGCOG2755.
HOGENOMHOG000261382.
KOK10804.
OMARGFPPQQ.
OrthoDBEOG6PGK4B.
PhylomeDBP0ADA1.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0ADA1.

Family and domain databases

Gene3D3.40.50.1110. 1 hit.
InterProIPR001087. Lipase_GDSL.
IPR008265. Lipase_GDSL_AS.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
PfamPF00657. Lipase_GDSL. 1 hit.
[Graphical view]
PROSITEPS01098. LIPASE_GDSL_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ADA1.
PROP0ADA1.

Entry information

Entry nameTESA_ECOLI
AccessionPrimary (citable) accession number: P0ADA1
Secondary accession number(s): P29679 expand/collapse secondary AC list , P37331, P77125, Q2MBT3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: June 11, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene