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

    Gene ID: 945877, updated on 17-Dec-2024

    Summary

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    Official Symbol
    btuC
    Official Full Name
    vitamin B12 ABC transporter membrane subunit
    Primary source
    ECOCYC:EG10127
    Locus tag
    b1711
    See related
    ASAP:ABE-0005712
    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].
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    Genomic context

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    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

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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. 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. 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
    4. 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
    5. Unravelling the folding and stability of an ABC (ATP-binding cassette) transporter. DiBartolo N, et al. Biochem Soc Trans, 2011 Jun. PMID 21599645

    See all (38) 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

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    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

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    Preferred Names
    vitamin B12 ABC transporter membrane subunit
    NP_416226.1

    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
      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

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