ID   BFRA_NEIMB              Reviewed;         154 AA.
AC   P0A0R1; P72080;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Bacterioferritin A;
DE            Short=BFR A;
DE            EC=1.16.3.1;
GN   Name=bfrA; OrderedLocusNames=NMB1207;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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   -!- 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:0000305};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC       {ECO:0000305};
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: 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; AE002098; AAF41589.1; -; Genomic_DNA.
DR   PIR; F81110; F81110.
DR   RefSeq; NP_274232.1; NC_003112.2.
DR   RefSeq; WP_002217177.1; NC_003112.2.
DR   AlphaFoldDB; P0A0R1; -.
DR   SMR; P0A0R1; -.
DR   STRING; 122586.NMB1207; -.
DR   PaxDb; 122586-NMB1207; -.
DR   GeneID; 66753132; -.
DR   KEGG; nme:NMB1207; -.
DR   PATRIC; fig|122586.8.peg.1514; -.
DR   HOGENOM; CLU_104506_2_0_4; -.
DR   InParanoid; P0A0R1; -.
DR   OrthoDB; 9800505at2; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR   GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
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   NCBIfam; TIGR00754; bfr; 1.
DR   PANTHER; PTHR30295; BACTERIOFERRITIN; 1.
DR   PANTHER; PTHR30295:SF9; BACTERIOFERRITIN; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   PIRSF; PIRSF002560; Bacterioferritin; 1.
DR   PRINTS; PR00601; BACFERRITIN.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00549; BACTERIOFERRITIN; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Iron storage; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..154
FT                   /note="Bacterioferritin A"
FT                   /id="PRO_0000192604"
FT   DOMAIN          1..145
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   BINDING         48
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         51
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         51
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         54
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         93
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         127
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         127
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         130
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   154 AA;  17961 MW;  15136D10DDA4346A CRC64;
     MQGNQAVVDY MNELLSGELA ARDQYFIHSR LYSEWGYTKL FERLNHEMEE ETTHAEDFIR
     RILMLGGTPK MARAELNIGT DVVSCLKADL QTEYEVRDAL KKGIKLCEEA QDYVTRDLMV
     AQLKDTEEDH AHWLEQQLRL IELIGEGNYY QSQL
//