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argS arginine--tRNA ligase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946452, updated on 2-May-2024

Summary

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Gene symbol
argS
Gene description
arginine--tRNA ligase
Primary source
ASAP:ABE-0006264
Locus tag
b1876
See related
ECOCYC:EG10071
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
ECK1877; lov; lov-1
Summary
ArgS 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: EG10071].
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Genomic context

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Sequence:
NC_000913.3 (1960062..1961795)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene PF03932 family protein CutC Neighboring gene putative metal-binding enzyme YecM Neighboring gene protein YecV Neighboring gene protein YecT

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. Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition. Bi K, et al. Protein Cell, 2014 Feb. PMID 24474195, Free PMC Article
  2. Crystallization and preliminary X-ray diffraction analysis of E. coli arginyl-tRNA synthetase in complex form with a tRNAArg. Zhou M, et al. Amino Acids, 2007. PMID 17061034
  3. Analysis of the kinetic mechanism of arginyl-tRNA synthetase. Airas RK. Biochim Biophys Acta, 2006 Feb. PMID 16427818
  4. Substrate-induced conformational changes in Escherichia coli arginyl-tRNA synthetase observed by 19F NMR spectroscopy. Yao YN, et al. FEBS Lett, 2003 Jul 17. PMID 12860413
  5. The Spectroscopic Study of E. coli Arginyl-tRNA Synthetase (ArgRS) and its Mutants. Gu WL, et al. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai), 1996. PMID 12232610

See all (36) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. 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.
  2. Combined with previously reported work on ArgRS, our results elucidated the structural and functional roles of a series of important residues in the active site, which furthered our understanding of this unique enzyme.
    Title: Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition.
  3. N-terminus verified by Edman degradation on complete protein
    Title: Isolation and characterization of the gene coding for Escherichia coli arginyl-tRNA synthetase.
  4. arginyl-tRNA synthetase (ArgRS) has been crystallized in complex form with tRNA(Arg) at pH 5.6; two crystal forms have been identified based on unit cell dimension
    Title: Crystallization and preliminary X-ray diffraction analysis of E. coli arginyl-tRNA synthetase in complex form with a tRNAArg.
Submit: New GeneRIF Correction

Pathways from PubChem

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General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables aminoacyl-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables arginine-tRNA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables arginine-tRNA ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables arginine-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in arginyl-tRNA aminoacylation IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within arginyl-tRNA aminoacylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in arginyl-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
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
arginine--tRNA ligase
NP_416390.1

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
    1960062..1961795
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416390.1 arginine--tRNA ligase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416390.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8T5Z9M9
    Conserved Domains (1) summary
    COG0018
    Location:1 → 577
    ArgS; Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]
Nucleotide Protein
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Gene LinkOut

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Other Literature Sources
Molecular Biology Databases
Research Materials