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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
    Heading Accession and Version

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    Other Literature Sources
    Molecular Biology Databases
    Research Materials