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O68926 (BFR_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 89. 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:STM3443
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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
Reference 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_0000192594

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
O68926 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 6D8145505FC59901

FASTA15818,355
        10         20         30         40         50         60 
MKGDVKIINY LNKLLGNELV AINQYFLHAR MFKNWGLTRL NDVEYHESID EMKHADKYIE 

        70         80         90        100        110        120 
RILFLEGIPN LQDLGKLGIG EDVEEMLRSD LRLELEGAKD LREAIAYADS VHDYVSRDMM 

       130        140        150 
IEILADEEGH IDWLETELDL IAKLGMQNYL QSQIKVTD 

« Hide

References

« Hide 'large scale' references
[1]Noorani S.M., Lindahl L., Zengel J.M.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF058449 Genomic DNA. Translation: AAC14283.1.
AE006468 Genomic DNA. Translation: AAL22306.1.
RefSeqNP_462347.1. NC_003197.1.

3D structure databases

ProteinModelPortalO68926.
SMRO68926. Positions 1-155.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM3443.

Proteomic databases

PaxDbO68926.
PRIDEO68926.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL22306; AAL22306; STM3443.
GeneID1254966.
KEGGstm:STM3443.
PATRIC32385685. VBISalEnt20916_3640.

Phylogenomic databases

eggNOGCOG2193.
HOGENOMHOG000262383.
KOK03594.
OMAEMKHADQ.
OrthoDBEOG6WDSKP.
ProtClustDBPRK10635.

Enzyme and pathway databases

BioCycSENT99287:GCTI-3465-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_SALTY
AccessionPrimary (citable) accession number: O68926
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 13, 2013
This is version 89 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