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

Gene ID: 945625, updated on 19-Feb-2025
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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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 Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

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. TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli. Pommier J, et al. J Biol Chem, 1998 Jun 26. PMID 9632735
  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
Products Interactant Other Gene Complex Source Pubs Description

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
  
involved_in protein maturation IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within protein maturation IEP
Inferred from Expression Pattern
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
  
Preferred Names
trimethylamine-N-oxide reductase-specific chaperone

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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
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