leuS leucine--tRNA ligase [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: leuS
Official Full Name: leucine--tRNA ligase
Primary source: ECOCYC:EG10532
Locus tag: b0642
See related: ASAP:ABE-0002196
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: ECK0635; syl
Summary: Leucyl-tRNA synthetase (LeuRS) is a member of the family of aminoacyl tRNA synthetases, which interpret the genetic code by covalently linking amino acids to their specific tRNA molecules. [More information is available at EcoCyc: EG10532].
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Genomic context

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Sequence:: NC_000913.3 (672201..674783, complement)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Mechanism of discrimination of isoleucyl-tRNA synthetase against nonproteinogenic alpha-aminobutyrate and its fluorinated analogues.
Title: Mechanism of discrimination of isoleucyl-tRNA synthetase against nonproteinogenic α-aminobutyrate and its fluorinated analogues.
Zinc is the molecular "switch" that controls the catalytic cycle of bacterial leucyl-tRNA synthetase
Title: Zinc is the molecular "switch" that controls the catalytic cycle of bacterial leucyl-tRNA synthetase.
In vitro assays showed that acetyl-phosphate nonenzymatically acetylates EcLeuRS and EcArgRS and suggested that the sirtuin class deacetylase CobB might regulate acetylation of these two enzymes. These findings imply a potential regulatory role for Lys acetylation in controlling the activity of aminoacyl-tRNA synthetases and thus protein synthesis.
Title: Acetylation of lysine ϵ-amino groups regulates aminoacyl-tRNA synthetase activity in Escherichia coli.
The prime biological function of LeuRS editing is to prevent mis-incorporation of the non-standard amino acid norvaline.
Title: The physiological target for LeuRS translational quality control is norvaline.
This work provides an assessment of how intra-molecular translocation of the tRNA CCA-tail balances the aminoacylation and editing activities of LeuRS.
Title: The Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation.
analysis of tRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase
Title: tRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase.
the functions of the CP2 domain are dependent on its location in the primary sequence of LeuRS
Title: The CP2 domain of leucyl-tRNA synthetase is crucial for amino acid activation and post-transfer editing.
A point mutation in CP1 of class I leucyl-tRNA synthetase inactivates deacylase activity and produces misacylated tRNA, although deletion of the entire CP1 domain also disabled the deacylase activity
Title: CP1-dependent partitioning of pretransfer and posttransfer editing in leucyl-tRNA synthetase.
identified specific residues within the beta-strand tethers that selectively impact enzyme activity, supporting the idea that beta-strand orientation is crucial for Leucyl-tRNA synthetase canonical core and CP1 domain functions
Title: Functional segregation of a predicted "hinge" site within the beta-strand linkers of Escherichia coli leucyl-tRNA synthetase.
Multiple nonstandard as well as standard amino acids were toxic to the cell when LeuRS editing was inactivated
Title: Amino acid toxicities of Escherichia coli that are prevented by leucyl-tRNA synthetase amino acid editing.

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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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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables aminoacyl-tRNA editing activity	IEA Inferred from Electronic Annotation more info
enables aminoacyl-tRNA ligase activity	IEA Inferred from Electronic Annotation more info
enables leucine-tRNA ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables leucine-tRNA ligase activity	IDA Inferred from Direct Assay more info	PubMed
enables leucine-tRNA ligase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in aminoacyl-tRNA metabolism involved in translational fidelity	IEA Inferred from Electronic Annotation more info
involved_in leucyl-tRNA aminoacylation	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within leucyl-tRNA aminoacylation	IDA Inferred from Direct Assay more info	PubMed
involved_in leucyl-tRNA aminoacylation	IEA Inferred from Electronic Annotation more info
involved_in tRNA aminoacylation for protein translation	IEA Inferred from Electronic Annotation more info
involved_in translation	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: leucine--tRNA ligase

NP_415175.1

EC 6.1.1.4

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

NC_000913.3 Reference assembly

Range

672201..674783 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_415175.1 leucine--tRNA ligase [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_415175.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A831GQJ8

Conserved Domains (1) summary

PRK00390
Location:1 → 860

leuS; leucyl-tRNA synthetase; Validated