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    torD trimethylamine-N-oxide reductase-specific chaperone [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945625, updated on 3-Dec-2024

    Summary

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    Official Symbol
    torD
    Official Full Name
    trimethylamine-N-oxide reductase-specific chaperone
    Primary source
    ECOCYC:EG12195
    Locus tag
    b0998
    See related
    ASAP:ABE-0003374
    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
    ECK0989
    Summary
    TorD prepares the molybdoenzyme TorA for MGD cofactor insertion, independent of signal peptide binding. torD, dmsD and ycdY are paralogs. [More information is available at EcoGene: EG12195]. TorD is encoded by the terminal open reading frame of the torCAD operon, which is involved in anaerobic respiration of trimethylamine N-oxide (TMAO) . [More information is available at EcoCyc: EG12195].
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    Genomic context

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    Sequence:
    NC_000913.3 (1061799..1062398)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene periplasmic trimethylamine-N-oxide binding protein Neighboring gene DNA-binding transcriptional dual regulator TorR Neighboring gene cytochrome c menaquinol dehydrogenase TorC Neighboring gene trimethylamine N-oxide reductase 1 Neighboring gene chaperone modulator CbpM Neighboring gene curved DNA-binding protein

    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. Intrinsic GTPase activity of a bacterial twin-arginine translocation proofreading chaperone induced by domain swapping. Guymer D, et al. FEBS J, 2010 Jan. PMID 20064164
    2. Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation. Bageshwar UK, et al. PLoS One, 2021. PMID 34499687, Free PMC Article
    3. The hydrophobic core of twin-arginine signal sequences orchestrates specific binding to Tat-pathway related chaperones. Shanmugham A, et al. PLoS One, 2012. PMID 22479549, Free PMC Article
    4. TorD, an essential chaperone for TorA molybdoenzyme maturation at high temperature. Genest O, et al. J Biol Chem, 2005 Apr 22. PMID 15723832
    5. Signal peptide-chaperone interactions on the twin-arginine protein transport pathway. Hatzixanthis K, et al. Proc Natl Acad Sci U S A, 2005 Jun 14. PMID 15941830, Free PMC Article

    See all (26) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.
      Title: Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.
    2. analysis of DmsD (specific for dimethylsulfoxide reductase, DmsA) and TorD (specific for trimethylamine N-oxide reductase, TorA).
      Title: The hydrophobic core of twin-arginine signal sequences orchestrates specific binding to Tat-pathway related chaperones.
    3. TorD binds tightly and with exquisite specificity to the TorA twin-arginine signal peptide in protein-targeting pathways.
      Title: Signal peptide-chaperone interactions on the twin-arginine protein transport pathway.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables molybdopterin cofactor binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables peptide binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in protein complex oligomerization IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein maturation IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    trimethylamine-N-oxide reductase-specific chaperone

    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
      1061799..1062398
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415518.1 trimethylamine-N-oxide reductase-specific chaperone [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415518.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8T6PQP3
      Conserved Domains (1) summary
      PRK04976
      Location:1 → 199
      torD; chaperone protein TorD; Validated
    Nucleotide Protein
    Heading Accession and Version

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