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btuD vitamin B12 ABC transporter ATP binding subunit [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945751, updated on 2-May-2024

Summary

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Gene symbol
btuD
Gene description
vitamin B12 ABC transporter ATP binding subunit
Primary source
ASAP:ABE-0005707
Locus tag
b1709
See related
ECOCYC:EG10128
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
ECK1707
Summary
BtuD is the ATP-binding component of the BtuCD, an ABC-type vitamin B12 uptake system. [More information is available at EcoCyc: EG10128].
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Genomic context

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Sequence:
NC_000913.3 (1792809..1793558, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene anti-FlhDC factor RflP Neighboring gene NlpC/P60 family lipoprotein NlpC Neighboring gene thioredoxin/glutathione peroxidase BtuE Neighboring gene vitamin B12 ABC transporter membrane subunit

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. 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
  2. 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
  3. Unravelling the folding and stability of an ABC (ATP-binding cassette) transporter. DiBartolo N, et al. Biochem Soc Trans, 2011 Jun. PMID 21599645
  4. 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
  5. The structure and function of drug pumps: an update. McKeegan KS, et al. Trends Microbiol, 2003 Jan. PMID 12526851

See all (37) 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. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
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Pathways from PubChem

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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 ABC-type vitamin B12 transporter activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables ABC-type vitamin B12 transporter activity IEA
Inferred from Electronic Annotation
more info
  
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables ATP binding ISM
Inferred from Sequence Model
more info
 PubMed 
enables ATP binding RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
enables ATP hydrolysis activity IEA
Inferred from Electronic Annotation
more info
  
enables ATPase-coupled transmembrane transporter activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
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
  
involved_in transmembrane transport IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
part_of ATP-binding cassette (ABC) transporter complex IBA
Inferred from Biological aspect of Ancestor
more info
  
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 extrinsic component of membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
vitamin B12 ABC transporter ATP binding subunit
NP_416224.1

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
    1792809..1793558 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416224.1 vitamin B12 ABC transporter ATP binding subunit [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416224.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A2X1KZC0, A0A376KWZ5, A0A403CSX7
    Conserved Domains (1) summary
    COG4138
    Location:2 → 249
    BtuD; ABC-type cobalamin transport system, ATPase component [Coenzyme transport and metabolism]
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

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Other Literature Sources
Molecular Biology Databases
Research Materials