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P0ADA2 (TESA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Ordered Locus Names:c0615
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Subunit structure

Monomer By similarity.

Subcellular location

Periplasm By similarity.

Sequence similarities

Belongs to the 'GDSL' lipolytic enzyme family.

Sequence caution

The sequence AAN79092.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionHydrolase
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlipid metabolic process

Inferred from electronic annotation. Source: InterPro

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlysophospholipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 208182Acyl-CoA thioesterase I
PRO_0000043365

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P0ADA2 [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

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
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.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN79092.1. Different initiation.
RefSeqNP_752548.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0ADA2.
SMRP0ADA2. Positions 27-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c0615.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN79092; AAN79092; c0615.
GeneID1036492.
KEGGecc:c0615.
PATRIC18279271. VBIEscCol75197_0580.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000261382.
KOK10804.
OMAPPNYGPD.
OrthoDBEOG6PGK4B.
ProtClustDBPRK10528.

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...

Entry information

Entry nameTESA_ECOL6
AccessionPrimary (citable) accession number: P0ADA2
Secondary accession number(s): P29679, P37331, P77125
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: November 13, 2013
This is version 54 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