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    lysS lysine--tRNA ligase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947372, updated on 3-Dec-2024

    Summary

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    Official Symbol
    lysS
    Official Full Name
    lysine--tRNA ligase
    Primary source
    ECOCYC:EG10552
    Locus tag
    b2890
    See related
    ASAP:ABE-0009486
    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
    asuD; ECK2885; herC
    Summary
    Mutants have reduced OM vesiculation (McBroom, 2006). [More information is available at EcoGene: EG10552]. The lysyl-tRNA synthetase LysS 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: EG10552].
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    Genomic context

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    Sequence:
    NC_000913.3 (3033657..3035174, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene uncharacterized protein YqfG Neighboring gene protein YqfH Neighboring gene isopentenyl-diphosphate Delta-isomerase Neighboring gene peptide chain release factor RF2 Neighboring gene ssDNA-specific exonuclease RecJ

    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. tRNA anticodon recognition and specification within subclass IIb aminoacyl-tRNA synthetases. Commans S, et al. J Mol Biol, 1998 May 15. PMID 9614943
    2. Isolation and characterization of herC, a mutation of Escherichia coli affecting maintenance of ColE1. Kawakami K, et al. Mol Gen Genet, 1989 Nov. PMID 2560134
    3. Mapping of the constitutive lysyl-tRNA synthetase gene of Escherichia coli K-12. Emmerich RV, et al. J Bacteriol, 1987 Nov. PMID 3312173, Free PMC Article
    4. Substrate recognition by class I lysyl-tRNA synthetases: a molecular basis for gene displacement. Ibba M, et al. Proc Natl Acad Sci U S A, 1999 Jan 19. PMID 9892648, Free PMC Article
    5. Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding. Onesti S, et al. Biochemistry, 2000 Oct 24. PMID 11041850

    See all (38) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. N-terminus verified by Edman degradation on mature peptide
      Title: Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species.
    Submit: New GeneRIF Correction

    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

    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 nucleic acid IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables lysine-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables lysine-tRNA ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables lysine-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables lysine-tRNA ligase activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables nucleic acid binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables tRNA binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Process Evidence Code Pubs
    involved_in lysyl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in lysyl-tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within lysyl-tRNA aminoacylation IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    acts_upstream_of_or_within tRNA aminoacylation for protein translation IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol HDA PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane HDA PubMed 

    General protein information

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    Preferred Names
    lysine--tRNA ligase
    NP_417366.1

    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
      3033657..3035174 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417366.1 lysine--tRNA ligase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417366.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376M341, A0A8S7RVU4
      Conserved Domains (1) summary
      PRK00484
      Location:14 → 503
      lysS; lysyl-tRNA synthetase; Reviewed
    Nucleotide Protein
    Heading Accession and Version

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