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

Summary

Gene symbol: tesA
Gene description: multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1
Primary source: ASAP:ABE-0001713
Locus tag: b0494
See related: ECOCYC:EG11542
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].
NEW: Try the new Gene table
Try the new Transcript table

NC_000913.3 Genomic Context describing neighboring genes

Go to nucleotide: Graphics FASTA GenBank

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.
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).
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.
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.
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

Function	Evidence Code	Pubs
enables arylesterase activity	IEA Inferred from Electronic Annotation more info
enables fatty acyl-CoA hydrolase activity	IDA Inferred from Direct Assay 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 hydrolase activity	IEA Inferred from Electronic Annotation more info
enables hydrolase activity, acting on ester bonds	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 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
enables phosphatidyl phospholipase B 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

Preferred Names: multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1

NP_415027.1

NEW Try the new Transcript table

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