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    bfr bacterioferritin [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947839, updated on 3-Dec-2024

    Summary

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    Official Symbol
    bfr
    Official Full Name
    bacterioferritin
    Primary source
    ECOCYC:EG10113
    Locus tag
    b3336
    See related
    ASAP:ABE-0010903
    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
    ECK3323
    Summary
    The bfr gene encodes bacterioferritin, which is an iron storage protein . [More information is available at EcoCyc: EG10113].
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    Genomic context

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    Sequence:
    NC_000913.3 (3466249..3466725, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene Type II secretion system protein GspL Neighboring gene Type II secretion system protein GspM Neighboring gene Type II secretion system prepilin peptidase Neighboring gene bacterioferritin-associated ferredoxin Neighboring gene endochitinase

    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. Spectroscopic studies of cobalt(II) binding to Escherichia coli bacterioferritin. Keech AM, et al. J Biol Chem, 1997 Jan 3. PMID 8995278
    2. Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua. Yang X, et al. Biochem J, 2000 Aug 1. PMID 10903139, Free PMC Article
    3. Intraabdominal desmoid tumor. Sy M, et al. JBR-BTR, 2000 Feb. PMID 10769510
    4. The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin. Yang X, et al. Biochemistry, 2000 Apr 25. PMID 10769150
    5. New fusion protein systems designed to give soluble expression in Escherichia coli. Davis GD, et al. Biotechnol Bioeng, 1999 Nov 20. PMID 10506413

    See all (61) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. these findings confirm that even a single charge-inversion mutation at the 2-fold interface of BFR can affect the quaternary structure of its dimers and their ability to self-assemble into cage structures.
      Title: Mutagenesis study to disrupt electrostatic interactions on the twofold symmetry interface of Escherichia coli bacterioferritin.
    2. Three computationally screened bioferritins are generated that present characterization of their stability and self assembly.
      Title: Stabilization of a protein nanocage through the plugging of a protein-protein interfacial water pocket.
    3. a large proportion of BFR core iron is released in the absence of a high affinity Fe(2+) chelator and further that chelators are not passive participants in iron release reactions
      Title: A new role for heme, facilitating release of iron from the bacterioferritin iron biomineral.
    4. the fluorescence intensity, due to the presence of two tryptophan residues (Trp35 and Trp133) in each of the 24 subunits, is highly sensitive to the iron status of the ferroxidase center and is quenched to different extents by Fe2+ and Fe3+
      Title: Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy.
    5. analysis of residues required for core formation in bacterioferritin
      Title: Structural and mechanistic studies of a stabilized subunit dimer variant of Escherichia coli bacterioferritin identify residues required for core formation.
    6. N-terminus verified by Edman degradation on complete protein
      Title: Amino acid sequence of the bacterioferritin (cytochrome b1) of Escherichia coli-K12.
    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 ferric iron binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ferrous iron transmembrane transporter activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ferroxidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ferroxidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ferroxidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables heme binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables heme binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables identical protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables iron ion binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables iron ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables iron ion sequestering activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in intracellular iron ion homeostasis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in intracellular sequestering of iron ion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in iron ion transmembrane transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in iron ion transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytosol HDA PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane HDA PubMed 

    General protein information

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    Preferred Names
    bacterioferritin
    NP_417795.1

    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
      3466249..3466725 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417795.1 bacterioferritin [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417795.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A377DBF7
      Conserved Domains (1) summary
      PRK10635
      Location:1 → 158
      PRK10635; bacterioferritin; Provisional
    Nucleotide Protein
    Heading Accession and Version

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