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

Gene ID: 947839, updated on 2-May-2024

Summary

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Gene symbol
bfr
Gene description
bacterioferritin
Primary source
ASAP:ABE-0010903
Locus tag
b3336
See related
ECOCYC:EG10113
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. Mutagenesis study to disrupt electrostatic interactions on the twofold symmetry interface of Escherichia coli bacterioferritin. Zhang Y, et al. J Biochem, 2015 Dec. PMID 26115686
  2. Stabilization of a protein nanocage through the plugging of a protein-protein interfacial water pocket. Ardejani MS, et al. Biochemistry, 2011 May 17. PMID 21488690
  3. A new role for heme, facilitating release of iron from the bacterioferritin iron biomineral. Yasmin S, et al. J Biol Chem, 2011 Feb 4. PMID 21106523, Free PMC Article
  4. Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy. Lawson TL, et al. Biochemistry, 2009 Sep 29. PMID 19705876
  5. Structural and mechanistic studies of a stabilized subunit dimer variant of Escherichia coli bacterioferritin identify residues required for core formation. Wong SG, et al. J Biol Chem, 2009 Jul 10. PMID 19439409, Free PMC Article

See all (62) 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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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ferric iron binding 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 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
    A0A5B9AU35
    Conserved Domains (1) summary
    PRK10635
    Location:1 → 158
    PRK10635; bacterioferritin; Provisional
Nucleotide Protein
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