ID   BFR_NITWI               Reviewed;          50 AA.
AC   P13570;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Bacterioferritin;
DE            Short=BFR;
DE            EC=1.16.3.1;
DE   AltName: Full=Cytochrome b-559;
DE   Flags: Fragment;
GN   Name=bfr;
OS   Nitrobacter winogradskyi (Nitrobacter agilis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=913;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 14123 / NBRC 14297 / NB-6-2;
RA   Kurokawa T., Fukumori Y., Yamanaka T.;
RT   "Nitrobacter winogradskyi cytochrome b-559: a nonhaem iron-containing
RT   cytochrome related to bacterioferritin.";
RL   Biochim. Biophys. Acta 976:135-139(1989).
CC   -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+)
CC       ions, oxidizes them by dioxygen to Fe(3+), and participates in the
CC       subsequent Fe(3+) oxide mineral core formation within the central
CC       cavity of the protein complex. {ECO:0000250}.
CC   -!- FUNCTION: May act as one of the electron carriers in the reverse
CC       electron-transport system from cytochrome c-552 to NADP(+).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC         Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC       {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 2 iron ions per subunit. The catalytic dinuclear iron-
CC       binding site within each subunit is known as the ferroxidase center.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Homooligomer of 24 subunits, arranged as 12 dimers, that are
CC       packed together to form an approximately spherical molecule with a
CC       central cavity, in which large amounts of iron can be deposited.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}.
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DR   PIR; A37394; A37394.
DR   AlphaFoldDB; P13570; -.
DR   SMR; P13570; -.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-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; 1.20.1260.10; -; 1.
DR   InterPro; IPR002024; Bacterioferritin.
DR   InterPro; IPR012347; Ferritin-like.
DR   InterPro; IPR009040; Ferritin-like_diiron.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR008331; Ferritin_DPS_dom.
DR   Pfam; PF00210; Ferritin; 1.
DR   PRINTS; PR00601; BACFERRITIN.
DR   SUPFAM; SSF47240; SSF47240; 1.
DR   PROSITE; PS00549; BACTERIOFERRITIN; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..>50
FT                   /note="Bacterioferritin"
FT                   /id="PRO_0000192609"
FT   DOMAIN          1..>50
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         18
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   NON_TER         50
SQ   SEQUENCE   50 AA;  6055 MW;  292E808421EA2919 CRC64;
     MKGDPKVIDY LNKALRHELT AINQYWLHYR LLDNWGIKDL AKKWRAESIE