ID   BFR_RHOCA               Reviewed;         161 AA.
AC   Q59738;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   05-APR-2011, entry version 60.
DE   RecName: Full=Bacterioferritin;
DE            Short=BFR;
GN   Name=bfr;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 938 / 37b4;
RX   MEDLINE=96275893; PubMed=8674981; DOI=10.1016/0378-1097(96)00133-4;
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 Fe(2+) to Fe(3+) before they are
CC       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; -; Genomic_DNA.
DR   PIR; S48182; S48182.
DR   PDB; 1JGC; X-ray; 2.60 A; A/B/C=1-161.
DR   PDBsum; 1JGC; -.
DR   ProteinModelPortal; Q59738; -.
DR   SMR; Q59738; 1-160.
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 process; 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   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   1: Evidence at protein level;
KW   3D-structure; Heme; Iron; Iron storage; Metal-binding.
FT   CHAIN         1    161       Bacterioferritin.
FT                                /FTId=PRO_0000192611.
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.
FT   HELIX         5     34
FT   HELIX        38     64
FT   HELIX        83    111
FT   HELIX       114    144
FT   HELIX       146    152
SQ   SEQUENCE   161 AA;  18173 MW;  9E534CBC531EC709 CRC64;
     MKGDAKVIEF LNAALRSELT AISQYWVHFR LQEDWGLAKM AKKSREESIE EMGHADKIIA
     RILFLEGHPN LQKLDPLRIG EGPRETLECD LAGEHDALKL YREARDYCAE VGDIVSKNIF
     ESLITDEEGH VDFLETQISL YDRLGPQGFA LLNAAPMDAA E
//