ID   BFR2_MAGMG              Reviewed;         160 AA.
AC   O50172;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Putative bacterioferritin subunit 2;
DE            Short=BFR 2;
GN   Name=bfr2;
OS   Magnetospirillum magnetotacticum (Aquaspirillum magnetotacticum).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31632 / DSM 3856 / NBRC 15272 / MS-1;
RX   PubMed=9409768; DOI=10.1016/s0378-1119(97)00424-1;
RA   Bertani L.E., Huang J.S., Weir B.A., Kirschvink J.L.;
RT   "Evidence for two types of subunits in the bacterioferritin of
RT   Magnetospirillum magnetotacticum.";
RL   Gene 201:31-36(1997).
CC   -!- FUNCTION: Iron-storage protein. {ECO:0000250}.
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   -!- SUBUNIT: Oligomer 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   EMBL; AF001959; AAC91254.1; -; Genomic_DNA.
DR   AlphaFoldDB; O50172; -.
DR   SMR; O50172; -.
DR   PRIDE; O50172; -.
DR   GO; GO:0008199; F:ferric iron binding; 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   CDD; cd00907; Bacterioferritin; 1.
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   PIRSF; PIRSF002560; Bacterioferritin; 1.
DR   PRINTS; PR00601; BACFERRITIN.
DR   SUPFAM; SSF47240; SSF47240; 1.
DR   TIGRFAMs; TIGR00754; bfr; 1.
DR   PROSITE; PS00549; BACTERIOFERRITIN; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Iron storage; Metal-binding.
FT   CHAIN           1..160
FT                   /note="Putative bacterioferritin subunit 2"
FT                   /id="PRO_0000192597"
FT   DOMAIN          1..145
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         51
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         52
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         130
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   160 AA;  18202 MW;  5E855893BE257099 CRC64;
     MKGDKEVLRH LNGVLKLHLT AINQYFLHAR MLKNWGLKDL GKAVYKYSIE EMKQADEVIE
     RILFLEGLPN LQDLGKLGIG EDVAEMLASD LKMEQAEHKA LTEAIALCET KQDFVTRDEL
     GEILEDTEEH IDWLETQIDL MAKMGTQNYL QAAMGQIEGD