ID   BFR_BRUSU               Reviewed;         161 AA.
AC   Q8FW95; G0KCU3;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-JAN-2012, entry version 52.
DE   RecName: Full=Bacterioferritin;
DE            Short=BFR;
DE            EC=1.16.3.1;
GN   Name=bfr; OrderedLocusNames=BRA0565, BS1330_II0560;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/JB.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
CC   -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds
CC       Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates
CC       in the subsequent Fe(3+) oxide mineral core formation within the
CC       central cavity of the protein complex (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer
CC       (By similarity).
CC   -!- COFACTOR: Binds 2 iron ions per subunit. The catalytic dinuclear
CC       iron-binding site within each subunit is known as the ferroxidase
CC       center (By similarity).
CC   -!- SUBUNIT: Homooligomer of 24 subunits, arranged as 12 dimers, that
CC       are packed together to form an approximately spherical molecule
CC       with a central cavity, in which large amounts of iron can be
CC       deposited (By similarity).
CC   -!- SIMILARITY: Belongs to the bacterioferritin family.
CC   -!- SIMILARITY: Contains 1 ferritin-like diiron domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE014292; AAN33754.1; -; Genomic_DNA.
DR   EMBL; CP002998; AEM20031.1; -; Genomic_DNA.
DR   RefSeq; NP_699749.1; NC_004311.2.
DR   ProteinModelPortal; Q8FW95; -.
DR   SMR; Q8FW95; 1-160.
DR   GeneID; 1165004; -.
DR   GenomeReviews; AE014292_GR; BRA0565.
DR   KEGG; bms:BRA0565; -.
DR   NMPDR; fig|204722.1.peg.2658; -.
DR   PATRIC; 17793933; VBIBruSui107850_2781.
DR   TIGR; BRA0565; -.
DR   HOGENOM; HBG288894; -.
DR   OMA; NMQVLDP; -.
DR   PhylomeDB; Q8FW95; -.
DR   ProtClustDB; CLSK864320; -.
DR   BioCyc; BSUI204722:BR_A0565-MONOMER; -.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:EC.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   InterPro; IPR002024; Bacterioferritin.
DR   InterPro; IPR009040; Ferritin-like.
DR   InterPro; IPR012347; Ferritin-rel.
DR   InterPro; IPR009078; Ferritin/RR-like.
DR   InterPro; IPR008331; Ferritin_DPS_dom.
DR   Gene3D; G3DSA:1.20.1260.10; Ferritin_rel; 1.
DR   KO; K03594; -.
DR   Pfam; PF00210; Ferritin; 1.
DR   PIRSF; PIRSF002560; Bacterioferritin; 1.
DR   PRINTS; PR00601; BACFERRITIN.
DR   SUPFAM; SSF47240; Ferritin/RR_like; 1.
DR   TIGRFAMs; TIGR00754; Bfr; 1.
DR   PROSITE; PS00549; BACTERIOFERRITIN; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Heme; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN         1    161       Bacterioferritin.
FT                                /FTId=PRO_0000192590.
FT   DOMAIN        1    145       Ferritin-like diiron.
FT   METAL        18     18       Iron 1 (By similarity).
FT   METAL        51     51       Iron 1 (By similarity).
FT   METAL        51     51       Iron 2 (By similarity).
FT   METAL        52     52       Iron (heme axial ligand); shared with
FT                                dimeric partner (By similarity).
FT   METAL        54     54       Iron 1 (By similarity).
FT   METAL        94     94       Iron 2 (By similarity).
FT   METAL       127    127       Iron 1 (By similarity).
FT   METAL       127    127       Iron 2 (By similarity).
FT   METAL       130    130       Iron 2 (By similarity).
SQ   SEQUENCE   161 AA;  18640 MW;  1D30A44BE843DDCE CRC64;
     MKGEPKVIER LNEALFLELG AVNQYWLHYR LLNDWGYTRL AKKEREESIE EMHHADKLID
     RIIFLEGFPN LQTVSPLRIG QNVKEVLEAD LKGEYDARAS YKESREICDK LGDYVSKQLF
     DELLADEEGH IDFLETQLDL LAKIGEERYG QLNAAPADEA E
//