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tesA multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1 [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945127, updated on 6-Jul-2026
Official Symbol
tesA
Official Full Name
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1
Primary source
ECOCYC:EG11542
Locus tag
b0494
See related
ASAP:ABE-0001713
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
apeA; ECK0488; pldC
Summary
The TAP complex (TesA) is a broad-specificity esterase that carries out thioesterase, arylesterase, lyophospholipase, and protease activities. [More information is available at EcoCyc: EG11542].
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Sequence:
NC_000913.3 (519139..519765, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative iron ABC exporter ATP-binding subunit FetA Neighboring gene putative iron ABC exporter membrane subunit FetB Neighboring gene chaperedoxin Neighboring gene NADP(+)-dependent aldehyde reductase YbbO Neighboring gene putative ABC transporter ATP-binding protein YbbA Neighboring gene putative ABC transporter membrane subunit YbbP Neighboring gene protein RhsD

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli. Lo YC, et al. Acta Crystallogr D Biol Crystallogr, 2000 Jun. PMID 10818355
  2. Detergent-resistant phospholipase A of Escherichia coli K-12. Purification and properties. Nishijima M, et al. Eur J Biochem, 1977 Feb 15. PMID 14002
  3. Protease I from Escherichia coli. Some physicochemical properties and substrate specificity. Pacaud M, et al. Eur J Biochem, 1976 Oct 1. PMID 791643
  4. Lysophospholipase L1 from Escherichia coli K-12 overproducer. Karasawa K, et al. J Biochem, 1991 Feb. PMID 1864840
  5. Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmityl thioesterase. Barnes EM Jr, et al. J Biol Chem, 1968 Jun 10. PMID 4871199

See all (26) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Structure-guided reshaping of the acyl binding pocket of 'TesA thioesterase enhances octanoic acid production in E. coli.
    Title: Structure-guided reshaping of the acyl binding pocket of 'TesA thioesterase enhances octanoic acid production in E. coli.
  2. conducted site-directed mutagenesis to change Trp into alanine (Ala), phenylalanine (Phe), or tyrosine (Tyr) to unveil the role of the Trp(23) indole ring
    Title: Functional role of a non-active site residue Trp(23) on the enzyme activity of Escherichia coli thioesterase I/protease I/lysophospholipase L(1).
  3. N-terminus verified by Edman degradation on mature peptide
    Title: Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of proteinase and proteinase-defective Escherichia coli mutants.
  4. Octanoic acid binding to the substrate-binding crevice of multifunctional tesA results in a continuous hydrophobic surface, which triggers switch loop movement essential for efficient catalysis of thioesters in tesA.
    Title: Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement.
  5. evaluated biochemical roles of amino acid residues in catalytic triad and oxyanion hole of Escherichia coli thioesterase I
    Title: Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables arylesterase activity EXP
Inferred from Experiment
more info
 PubMed 
enables arylesterase activity IEA
Inferred from Electronic Annotation
more info
  
enables carboxylesterase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables carboxylesterase activity IEA
Inferred from Electronic Annotation
more info
  
enables fatty acyl-CoA hydrolase activity EXP
Inferred from Experiment
more info
 PubMed 
enables fatty acyl-CoA hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables fatty acyl-[ACP] hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables lipase activity IEA
Inferred from Electronic Annotation
more info
  
enables long-chain fatty acyl-CoA hydrolase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables long-chain fatty acyl-CoA hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables medium-chain fatty acyl-CoA hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables phosphatidylcholine lysophospholipase A1 activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables phosphatidylcholine lysophospholipase A1 activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables phosphatidylcholine lysophospholipase A1 activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in lipid catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in lipid metabolic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in outer membrane-bounded periplasmic space IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in outer membrane-bounded periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in periplasmic space EXP
Inferred from Experiment
more info
 PubMed 
located_in periplasmic space IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1
NP_415027.1

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    519139..519765 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415027.1 multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1

    See identical proteins and their annotated locations for NP_415027.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A0H3EGR5, B7UKH7
    Conserved Domains (1) summary
    PRK10528
    Location:18 → 208
    PRK10528; multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
Nucleotide Protein
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