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P45430 (BFR_MYCPA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 94. 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):
Antigen D
Gene names
Name:bfr
Synonyms:bfrA
Ordered Locus Names:MAP_1595
OrganismMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) [Complete proteome] [HAMAP]
Taxonomic identifier262316 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length159 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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
Direct protein sequencing
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 – 159159Bacterioferritin
PRO_0000192602

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
P45430 [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: 65BEF1425437EEBA

FASTA15918,479
        10         20         30         40         50         60 
MQGDPEVLRL LNEQLTSELT AINQYFLHSK MQDNWGFTEL AEHTRAESFD EMRHAEAITD 

        70         80         90        100        110        120 
RILLLDGLPN YQRLFSLRIG QTLREQFEAD LAIEYEVMDR LKPAIILCRE KQDSTTATLF 

       130        140        150 
EQIVADEEKH IDYLETQLEL MDKLGVELYS AQCVSRPPS 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.
[2]"Mycobacterium paratuberculosis antigen D: characterization and evidence that it is a bacterioferritin."
Brooks B.W., Young N.M., Watson D.C., Robertson R.H., Sugden E.A., Nielsen K.H., Becker S.A.
J. Clin. Microbiol. 29:1652-1658(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-42.
Strain: C-286.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016958 Genomic DNA. Translation: AAS03912.1.
PIRA44893.
RefSeqNP_960529.1. NC_002944.2.

3D structure databases

ProteinModelPortalP45430.
SMRP45430. Positions 1-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262316.MAP1595.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS03912; AAS03912; MAP_1595.
GeneID2718534.
KEGGmpa:MAP1595.
PATRIC17995720. VBIMycAvi108102_1688.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2193.
KOK03594.
OMAEMKHADQ.
OrthoDBEOG6WDSKP.
ProtClustDBCLSK791451.

Enzyme and pathway databases

BioCycMAVI262316:GCQR-1617-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_MYCPA
AccessionPrimary (citable) accession number: P45430
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: March 15, 2004
Last modified: November 13, 2013
This is version 94 of the entry and version 2 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