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P0ABD4 (BFR_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bacterioferritin

Short name=BFR
EC=1.16.3.1
Alternative name(s):
Cytochrome b-1
Cytochrome b-557
Gene names
Name:bfr
Ordered Locus Names:c4107
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Iron-storage protein, whose ferroxidase center binds Fe2+ ions, oxidizes them by dioxygen to Fe3+, and participates in the subsequent Fe3+ oxide mineral core formation within the central cavity of the protein complex By similarity.

Catalytic activity

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity.

Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center By similarity.

Subunit structure

Homooligomer of 24 subunits, arranged as 12 dimers, that are packed together to form an approximately spherical molecule with a central cavity, in which large amounts of iron can be deposited By similarity.

Sequence similarities

Belongs to the bacterioferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
   Biological processIron storage
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellular iron ion homeostasis

Inferred from electronic annotation. Source: UniProtKB-KW

iron ion transport

Inferred from electronic annotation. Source: InterPro

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

ferroxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158Bacterioferritin
PRO_0000192593

Regions

Domain1 – 145145Ferritin-like diiron

Sites

Metal binding181Iron 1 By similarity
Metal binding511Iron 1 By similarity
Metal binding511Iron 2 By similarity
Metal binding521Iron (heme axial ligand); shared with dimeric partner By similarity
Metal binding541Iron 1 By similarity
Metal binding941Iron 2 By similarity
Metal binding1271Iron 1 By similarity
Metal binding1271Iron 2 By similarity
Metal binding1301Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P0ABD4 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: A6C86CE1CD8F865A

FASTA15818,495
        10         20         30         40         50         60 
MKGDTKVINY LNKLLGNELV AINQYFLHAR MFKNWGLKRL NDVEYHESID EMKHADRYIE 

        70         80         90        100        110        120 
RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LALELDGAKN LREAIGYADS VHDYVSRDMM 

       130        140        150 
IEILRDEEGH IDWLETELDL IQKMGLQNYL QAQIREEG 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN82545.1.
RefSeqNP_755971.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0ABD4.
SMRP0ABD4. Positions 1-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c4107.

Proteomic databases

PRIDEP0ABD4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN82545; AAN82545; c4107.
GeneID1036151.
KEGGecc:c4107.
PATRIC18285968. VBIEscCol75197_3860.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000262383.
KOK03594.
OMAEMKHADQ.
OrthoDBEOG6WDSKP.
ProtClustDBPRK10635.

Enzyme and pathway databases

BioCycECOL199310:C4107-MONOMER.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFPIRSF002560. Bacterioferritin. 1 hit.
PRINTSPR00601. BACFERRITIN.
SUPFAMSSF47240. SSF47240. 1 hit.
TIGRFAMsTIGR00754. bfr. 1 hit.
PROSITEPS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBFR_ECOL6
AccessionPrimary (citable) accession number: P0ABD4
Secondary accession number(s): O68931, P11056
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: December 11, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families