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   03-OCT-2012, entry version 68.
DE   RecName: Full=Bacterioferritin;
DE            Short=BFR;
DE            EC=1.16.3.1;
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: 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   -!- COFACTOR: Binds 2 iron ions per subunit. The catalytic dinuclear
CC       iron-binding site within each subunit is known as the ferroxidase
CC       center.
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.
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   HOGENOM; HOG000262383; -.
DR   EvolutionaryTrace; Q59738; -.
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   Gene3D; G3DSA:1.20.1260.10; Ferritin_rel; 1.
DR   InterPro; IPR002024; Bacterioferritin.
DR   InterPro; IPR009040; Ferritin-like_diiron.
DR   InterPro; IPR012347; Ferritin-rel.
DR   InterPro; IPR009078; Ferritin/RNR-like.
DR   InterPro; IPR008331; Ferritin_DPS_dom.
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; Oxidoreductase.
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); shared with
FT                                dimeric partner.
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
//