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    hisS histidine--tRNA ligase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946989, updated on 3-Dec-2024

    Summary

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    Official Symbol
    hisS
    Official Full Name
    histidine--tRNA ligase
    Primary source
    ECOCYC:EG10453
    Locus tag
    b2514
    See related
    ASAP:ABE-0008278
    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
    ECK2510
    Summary
    Histidyl-tRNA synthetase (HisRS) 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: EG10453].
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    Genomic context

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    Sequence:
    NC_000913.3 (2639301..2640575, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene outer membrane protein assembly factor BamB Neighboring gene ancillary SecYEG translocon subunit Neighboring gene ncRNA Neighboring gene (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin)

    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. Asymmetric amino acid activation by class II histidyl-tRNA synthetase from Escherichia coli. Guth E, et al. J Biol Chem, 2009 Jul 31. PMID 19487703, Free PMC Article
    2. Purification and characterization of histidyl transfer ribonucleic acid synthetase of Escherichia coli. Kalousek F, et al. Biochemistry, 1974 Feb 26. PMID 4591623
    3. The nucleotide sequence of the promoter region of hisS, the structural gene for histidyl-tRNA synthetase. Eisenbeis SJ, et al. Gene, 1982 May. PMID 6290315
    4. Strains of Escherichia coli carrying the structural gene for histidyl-tRNA synthetase on a high copy-number plasmid. Eisenbeis SJ, et al. Mol Gen Genet, 1981. PMID 6460151
    5. Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate. Arnez JG, et al. EMBO J, 1995 Sep 1. PMID 7556055, Free PMC Article

    See all (35) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. N-terminus verified by Edman degradation on mature peptide
      Title: Primary structure of histidine-tRNA synthetase and characterization of hisS transcripts.
    2. Surprising conclusion from study of concerted, substrate assisted mechanism of aminoacylation by histidyl-tRNA synthetase is that the overall rate of aminoacylation is slower than individual rates of either amino acid activation or aminoacyl transfer.
      Title: A substrate-assisted concerted mechanism for aminoacylation by a class II aminoacyl-tRNA synthetase.
    3. By use of a rapid kinetics analysis employing mutants in tRNA(His) and its cognate aminoacyl-tRNA synthetase, the role of tRNA identity in aminoacylation was investigated.
      Title: Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    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 catalytic activity, acting on a tRNA IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables histidine-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables histidine-tRNA ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables histidine-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in histidyl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within histidyl-tRNA aminoacylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in histidyl-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
    histidine--tRNA ligase
    NP_417009.1

    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
      2639301..2640575 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417009.1 histidine--tRNA ligase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417009.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2W6PA59
      Conserved Domains (1) summary
      PRK00037
      Location:4 → 424
      hisS; histidyl-tRNA synthetase; Reviewed
    Nucleotide Protein
    Heading Accession and Version

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