U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

torC cytochrome c menaquinol dehydrogenase TorC [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946252, updated on 4-Apr-2024

Summary

Go to the top of the page Help
Gene symbol
torC
Gene description
cytochrome c menaquinol dehydrogenase TorC
Primary source
ASAP:ABE-0003370
Locus tag
b0996
See related
ECOCYC:EG11815
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
ECK0987
Summary
TorC is a pentahemic c-type cytochrome that is anchored to the inner membrane. [More information is available at EcoCyc: EG11815].
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
Sequence:
NC_000913.3 (1058084..1059256)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene sensor histidine kinase TorS Neighboring gene periplasmic trimethylamine-N-oxide binding protein Neighboring gene DNA-binding transcriptional dual regulator TorR Neighboring gene trimethylamine N-oxide reductase 1 Neighboring gene trimethylamine-N-oxide reductase-specific chaperone Neighboring gene chaperone modulator CbpM Neighboring gene curved DNA-binding protein

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Aerobic TMAO respiration in Escherichia coli. Ansaldi M, et al. Mol Microbiol, 2007 Oct. PMID 17850256
  2. TorC apocytochrome negatively autoregulates the trimethylamine N-oxide (TMAO) reductase operon in Escherichia coli. Ansaldi M, et al. Mol Microbiol, 1999 Jul. PMID 10411745
  3. Bacterial reduction of trimethylamine oxide. Barrett EL, et al. Annu Rev Microbiol, 1985. PMID 3904597
  4. Further characterization of trimethylamine N-oxide reductase from Escherichia coli, a molybdoprotein. Yamamoto I, et al. J Biochem, 1986 Jun. PMID 3528139
  5. The inducible trimethylamine-N-oxide reductase of Escherichia coli K12: biochemical and immunological studies. Silvestro A, et al. Biochim Biophys Acta, 1988 Apr 28. PMID 3282544

See all (23) citations in PubMed

GeneRIFs: Gene References Into Functions

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables electron transfer activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables electron transfer activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables electron transfer activity IEA
Inferred from Electronic Annotation
more info
  
enables heme binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables heme binding IEA
Inferred from Electronic Annotation
more info
  
enables heme binding ISM
Inferred from Sequence Model
more info
 PubMed 
enables iron ion binding IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in aerobic respiration IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within aerobic respiration IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within anaerobic electron transport chain IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in anaerobic electron transport chain IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in anaerobic respiration IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in anaerobic respiration IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within anaerobic respiration IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within negative regulation of signal transduction IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in regulation of pH IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in Gram-negative-bacterium-type cell wall IEA
Inferred from Electronic Annotation
more info
  
located_in membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
located_in membrane ISM
Inferred from Sequence Model
more info
 PubMed 
located_in outer membrane-bounded periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
part_of trimethylamine-N-oxide reductase (cytochrome c) complex IPI
Inferred from Physical Interaction
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
cytochrome c menaquinol dehydrogenase TorC

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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
    1058084..1059256
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415516.1 cytochrome c menaquinol dehydrogenase TorC [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415516.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A0H2V6R0, A0A192CLE3, A0AA36KW37, Q1RDM0
    Conserved Domains (1) summary
    PRK15032
    Location:1 → 390
    PRK15032; pentaheme c-type cytochrome TorC
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.