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    mnmE 5-carboxymethylaminomethyluridine-tRNA synthase GTPase subunit [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948222, updated on 3-Dec-2024

    Summary

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    Official Symbol
    mnmE
    Official Full Name
    5-carboxymethylaminomethyluridine-tRNA synthase GTPase subunit
    Primary source
    ECOCYC:EG10997
    Locus tag
    b3706
    See related
    ASAP:ABE-0012123
    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
    ECK3699; thdF; trmE
    Summary
    GTPase activity is essential for modification function. [More information is available at EcoGene: EG10997]. MnmE is required for wild-type 5-methylaminomethyl-2-thiouridine modification of tRNA . [More information is available at EcoCyc: EG10997].
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    Genomic context

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    Sequence:
    NC_000913.3 (3886828..3888192)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene RNase P protein component Neighboring gene membrane protein insertion efficiency factor Neighboring gene membrane protein insertase YidC Neighboring gene tnaAB operon leader peptide Neighboring gene tryptophanase

    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. Effects of mutagenesis in the switch I region and conserved arginines of Escherichia coli MnmE protein, a GTPase involved in tRNA modification. Martínez-Vicente M, et al. J Biol Chem, 2005 Sep 2. PMID 15983041
    2. Molecular cloning and sequence of the thdF gene, which is involved in thiophene and furan oxidation by Escherichia coli. Alam KY, et al. J Bacteriol, 1991 Oct. PMID 1917835, Free PMC Article
    3. Regulation of the thdF gene, which is involved in thiophene oxidation by Escherichia coli K-12. Zabel MD, et al. Microbios, 2000. PMID 10738982
    4. The GTPase activity and C-terminal cysteine of the Escherichia coli MnmE protein are essential for its tRNA modifying function. Yim L, et al. J Biol Chem, 2003 Aug 1. PMID 12730230
    5. Backbone 1H, 13C and 15N resonance assignments for the 18.7 kDa GTPase domain of Escherichia coli MnmE protein. Monleón D, et al. J Biomol NMR, 2004 Mar. PMID 14752268

    See all (44) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. deletion of the mnmE or mnmG gene results in complete inhibition of growth unless the medium contains polyamines
      Title: Absolute requirement for polyamines for growth of Escherichia coli mutants (mnmE/G) defective in modification of the wobble anticodon of transfer-RNA.
    2. The uridylyltransferase GlnD and tRNA modification GTPase MnmE allosterically control Escherichia coli folylpoly-gamma-glutamate synthase FolC.
      Title: The uridylyltransferase GlnD and tRNA modification GTPase MnmE allosterically control Escherichia coli folylpoly-γ-glutamate synthase FolC.
    3. Investigation of the activities and the tRNA specificity of the MnmE enzyme.
      Title: The output of the tRNA modification pathways controlled by the Escherichia coli MnmEG and MnmC enzymes depends on the growth conditions and the tRNA species.
    4. GidA binding induces large conformational and dynamic changes in MnmE
      Title: Stabilization of G domain conformations in the tRNA-modifying MnmE-GidA complex observed with double electron electron resonance spectroscopy.
    5. The MnmE*GidA complex catalyzes two different GTP- and FAD-dependent reactions, which produce 5-aminomethyluridine and 5-carboxymethylamino-methyluridine using ammonium and glycine, respectively, as substrates.
      Title: Evolutionarily conserved proteins MnmE and GidA catalyze the formation of two methyluridine derivatives at tRNA wobble positions.
    6. Hydrolysis of GTP and intact complex formation in the MnmE-GidA complex is essential for the in vitro and in in vivo tRNA-modification activity which employs glycine as a substrate.
      Title: G-domain dimerization orchestrates the tRNA wobble modification reaction in the MnmE/GidA complex.
    7. Biochemical and X-ray structural evidence provided for a new GTP-hydrolysis mechanism, where the G-domains of MnmE dimerise in a potassium-dependent manner and induce GTP hydrolysis.
      Title: Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element.
    8. Mutational analysis of all conserved arginine residues of the MnmE G-domain indicates that MnmE, unlike other GTPases, does not use an arginine finger to drive catalysis.
      Title: Effects of mutagenesis in the switch I region and conserved arginines of Escherichia coli MnmE protein, a GTPase involved in tRNA modification.
    9. Data suggest that TrmE is part of an increasingly complex control network designed to integrate diverse physiological signals and forecast future exposures to extreme acid.
      Title: The Era-like GTPase TrmE conditionally activates gadE and glutamate-dependent acid resistance in Escherichia coli.
    10. MnmE and GidA form a functional complex in the tRNA modification process in which both proteins are interdependent.
      Title: Further insights into the tRNA modification process controlled by proteins MnmE and GidA of Escherichia coli.
    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 GDP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables GTP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables GTP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables GTPase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables GTPase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables potassium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within chaperone-mediated protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in regulation of cytoplasmic translational fidelity NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    acts_upstream_of_or_within response to pH IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tRNA methylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within tRNA methylation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tRNA modification IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in tRNA wobble uridine modification IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within tRNA wobble uridine modification IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within tRNA wobble uridine modification IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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 
    part_of cytosolic tRNA wobble base thiouridylase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    5-carboxymethylaminomethyluridine-tRNA synthase GTPase subunit

    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
      3886828..3888192
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418162.1 5-carboxymethylaminomethyluridine-tRNA synthase GTPase subunit [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418162.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7RYS3
      Conserved Domains (1) summary
      PRK05291
      Location:1 → 454
      trmE; tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE
    Nucleotide Protein
    Heading Accession and Version

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