ID   BFR_RHOCA      STANDARD;      PRT;   161 AA.
AC   Q59738;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Bacterioferritin (BFR).
GN   Name=bfr;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=DSM 938 / 37b4;
RX   MEDLINE=96275893; PubMed=8674981;
RA   Penfold C.N., Ringeling P.L., Davy S.L., Moore G.R., McEwan A.G.,
RA   Spiro S.;
RT   "Isolation, characterisation and expression of the bacterioferritin
RT   gene of Rhodobacter capsulatus.";
RL   FEMS Microbiol. Lett. 139:143-148(1996).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   MEDLINE=21620770; PubMed=11752777;
RA   Cobessi D., Huang L.-S., Ban M., Pon N.G., Daldal F., Berry E.A.;
RT   "The 2.6 A resolution structure of Rhodobacter capsulatus
RT   bacterioferritin with metal-free dinuclear site and heme iron in a
RT   crystallographic 'special position'.";
RL   Acta Crystallogr. D 58:29-38(2002).
CC   -!- FUNCTION: May perform analogous functions in iron detoxification
CC       and storage to that of animal ferritins (By similarity).
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer.
CC   -!- SUBUNIT: Oligomer of 24 identical subunits.
CC   -!- MISCELLANEOUS: The di-iron binding site functions as active site
CC       where iron ions are oxidized from iron(II) to iron(III) before
CC       they are stored.
CC   -!- SIMILARITY: Belongs to the bacterioferritin family.
CC   -!- SIMILARITY: Contains 1 ferritin-like diiron domain.
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DR   EMBL; Z54247; CAA91017.1; -.
DR   PDB; 1JGC; 09-JAN-02.
DR   InterPro; IPR002024; Bacterioferritin.
DR   InterPro; IPR009078; Ferritin/RR_like.
DR   InterPro; IPR008331; Ferritin_Dps.
DR   InterPro; IPR009040; Ferritin_like.
DR   Pfam; PF00210; Ferritin; 1.
DR   PRINTS; PR00601; BACFERRITIN.
DR   ProDom; PD002269; Bacterioferritin; 1.
DR   TIGRFAMs; TIGR00754; bfr; 1.
DR   PROSITE; PS00549; BACTERIOFERRITIN; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
KW   Iron storage; Heme; Metal-binding; Iron; 3D-structure.
FT   DOMAIN        1    145       Ferritin-like diiron.
FT   METAL        18     18       Iron 1.
FT   METAL        51     51       Iron 1.
FT   METAL        51     51       Iron 2.
FT   METAL        52     52       Iron (heme axial ligand).
FT   METAL        54     54       Iron 1.
FT   METAL        94     94       Iron 2.
FT   METAL       127    127       Iron 1.
FT   METAL       127    127       Iron 2.
FT   METAL       130    130       Iron 2.
SQ   SEQUENCE   161 AA;  18172 MW;  9E534CBC531EC709 CRC64;
     MKGDAKVIEF LNAALRSELT AISQYWVHFR LQEDWGLAKM AKKSREESIE EMGHADKIIA
     RILFLEGHPN LQKLDPLRIG EGPRETLECD LAGEHDALKL YREARDYCAE VGDIVSKNIF
     ESLITDEEGH VDFLETQISL YDRLGPQGFA LLNAAPMDAA E
//