U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

btuC vitamin B12 ABC transporter membrane subunit [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945877, updated on 11-Apr-2024

Summary

Go to the top of the page Help
Gene symbol
btuC
Gene description
vitamin B12 ABC transporter membrane subunit
Primary source
ASAP:ABE-0005712
Locus tag
b1711
See related
ECOCYC:EG10127
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
ECK1709
Summary
BtuC is the integral membrane component of BtuCD, an ABC type vitamin B12 uptake system. [More information is available at EcoCyc: EG10127].
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 (1794172..1795152, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene vitamin B12 ABC transporter ATP binding subunit Neighboring gene thioredoxin/glutathione peroxidase BtuE Neighboring gene integration host factor subunit alpha Neighboring gene phenylalanine--tRNA ligase subunit beta

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. A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization. Tal N, et al. Proc Natl Acad Sci U S A, 2013 Apr 2. PMID 23513227, Free PMC Article
  2. ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations. Pan C, et al. PLoS One, 2016. PMID 27870912, Free PMC Article
  3. The conformational transition pathways of ATP-binding cassette transporter BtuCD revealed by targeted molecular dynamics simulation. Weng J, et al. PLoS One, 2012. PMID 22272354, Free PMC Article
  4. Unravelling the folding and stability of an ABC (ATP-binding cassette) transporter. DiBartolo N, et al. Biochem Soc Trans, 2011 Jun. PMID 21599645
  5. Conformational transitions induced by the binding of MgATP to the vitamin B12 ATP-binding cassette (ABC) transporter BtuCD. Oloo EO, et al. J Biol Chem, 2004 Oct 22. PMID 15308647

See all (39) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The periplasmic soluble binding protein BtuF binds the vitamin B12 and the transmembrane and ATPase domains BtuCD mediate the translocation.
    Title: Single-molecule visualization of conformational changes and substrate transport in the vitamin B(12) ABC importer BtuCD-F.
  2. study used molecular dynamics simulations to investigate the atomic-level mechanism of conformational coupling in the ABC transporter BtuCD-F
    Title: Release of Entropic Spring Reveals Conformational Coupling Mechanism in the ABC Transporter BtuCD-F.
  3. ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations
    Title: ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations.
  4. A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization.
    Title: A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization.
  5. Data suggest that the asymmetric crystal structure of BtuCD-F is an intermediate state in the process of reverse inward-facing to outward-facing (I-->O) transition.
    Title: The conformational transition pathways of ATP-binding cassette transporter BtuCD revealed by targeted molecular dynamics simulation.
  6. Data suggest that BtuF does not discriminate between, or impose, asymmetric conformations of BtuC/BtuD complex. Data confirm conformational disorder observed in BtuC/BtuD/BtuF crystals.
    Title: Asymmetric states of vitamin B₁₂ transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF.
  7. Data provide insights into the subunit interactions of an ABC transporter and lays the foundation for studies of the reassembly of BtuCD.
    Title: Unravelling the folding and stability of an ABC (ATP-binding cassette) transporter.
  8. ATP-binding cassette transporter BtuCD mediating vitamin B(12) uptake in Escherichia coli couples the energy of ATP hydrolysis to the translocation of vitamin B(12) across the membrane into the cell.
    Title: The conformational coupling and translocation mechanism of vitamin B12 ATP-binding cassette transporter BtuCD.
  9. The 2.6 angstrom crystal structure of a complex BtuCD-F reveals substantial conformational changes as compared with the previously reported structures of BtuCD and BtuF
    Title: Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF.
Submit: New GeneRIF Correction

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 ABC-type vitamin B12 transporter activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables transmembrane transporter activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables transmembrane transporter activity IEA
Inferred from Electronic Annotation
more info
  
enables vitamin transmembrane transporter activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in cobalamin transport IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within cobalamin transport IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in cobalamin transport IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in cobalamin transport IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within cobalamin transport IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in transmembrane transport IEA
Inferred from Electronic Annotation
more info
  
involved_in vitamin transmembrane transport IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
part_of ATP-binding cassette (ABC) transporter complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of BtuCD complex IPI
Inferred from Physical Interaction
more info
 PubMed 
part_of cobalamin transport complex IPI
Inferred from Physical Interaction
more info
 PubMed 
located_in membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
is_active_in plasma membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

Go to the top of the page Help
Preferred Names
vitamin B12 ABC transporter membrane subunit
NP_416226.1

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
    1794172..1795152 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416226.1 vitamin B12 ABC transporter membrane subunit [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416226.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A376S8K3, A0A5B9AM81
    Conserved Domains (1) summary
    PRK03784
    Location:1 → 326
    PRK03784; vtamin B12-transporter permease; Provisional
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.

Other Literature Sources
Molecular Biology Databases
Research Materials