ID   BFR_BRUSU               Reviewed;         161 AA.
AC   Q8FW95;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   09-FEB-2010, entry version 40.
DE   RecName: Full=Bacterioferritin;
DE            Short=BFR;
GN   Name=bfr; OrderedLocusNames=BRA0565;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
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).
CC   -!- FUNCTION: May perform analogous functions in iron detoxification
CC       and storage to that of animal ferritins.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer
CC       (By similarity).
CC   -!- SUBUNIT: Oligomer of 24 identical subunits (By similarity).
CC   -!- MISCELLANEOUS: The di-iron binding site functions as active site
CC       where iron ions are oxidized from Fe(2+) to Fe(3+) before they are
CC       stored (By similarity).
CC   -!- SIMILARITY: Belongs to the bacterioferritin family.
CC   -!- SIMILARITY: Contains 1 ferritin-like diiron domain.
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DR   EMBL; AE014292; AAN33754.1; -; Genomic_DNA.
DR   RefSeq; NP_699749.1; -.
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   TIGR; BRA0565; -.
DR   HOGENOM; HBG288894; -.
DR   OMA; FLDGFPN; -.
DR   PhylomeDB; Q8FW95; -.
DR   BioCyc; BSUI204722:BR_A0565-MONOMER; -.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:InterPro.
DR   InterPro; IPR002024; Bacterioferritin.
DR   InterPro; IPR009040; Ferritin-like.
DR   InterPro; IPR009078; Ferritin/RR-like.
DR   InterPro; IPR008331; Ferritin_Dps.
DR   InterPro; IPR012347; Ferritin_rel.
DR   Gene3D; G3DSA:1.20.1260.10; Ferritin_rel; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   PIRSF; PIRSF002560; Bacterioferritin; 1.
DR   PRINTS; PR00601; BACFERRITIN.
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.
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) (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
//