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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 17-Dec-2024

    Summary

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    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
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; 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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    Genomic context

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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 regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    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

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables arylesterase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables carboxylic ester hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 lysophospholipase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables lysophospholipase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables lysophospholipase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in lipid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in outer membrane-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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

    NCBI Reference Sequences (RefSeq)

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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 [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415027.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A0H3EGR5, A0A266HY79, A0A2H4TPG9, A0A3L5GXW7, A0A6M7H1J3, A0A826IW41, B7MQL2, B7N955, B7UKH7, C3TKZ7
      Conserved Domains (1) summary
      PRK10528
      Location:18 → 208
      PRK10528; multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
    Nucleotide Protein
    Heading Accession and Version

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