ID   BFRB_MYCTO              Reviewed;         181 AA.
AC   P9WNE4; L0TGW6; P96237; Q7BS08; Q7D4R7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Ferritin BfrB;
DE            EC=1.16.3.1;
DE   AltName: Full=Non-heme ferritin Ftn;
DE   AltName: Full=Nox19;
GN   Name=bfrB; Synonyms=ftn; OrderedLocusNames=MT3949;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Iron-storage protein that displays ferroxidase activity,
CC       catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then
CC       be deposited as a ferric-oxide mineral core within the central cavity
CC       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   -!- SUBUNIT: Homooligomer of 24 subunits that are packed together to form
CC       an approximately spherical molecule with a central cavity, in which
CC       large amounts of iron can be stored. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK48316.1; -; Genomic_DNA.
DR   PIR; F70653; F70653.
DR   RefSeq; WP_003420920.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNE4; -.
DR   SMR; P9WNE4; -.
DR   EnsemblBacteria; AAK48316; AAK48316; MT3949.
DR   GeneID; 45427842; -.
DR   KEGG; mtc:MT3949; -.
DR   PATRIC; fig|83331.31.peg.4247; -.
DR   HOGENOM; CLU_065681_1_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
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   CDD; cd01055; Nonheme_Ferritin; 1.
DR   Gene3D; 1.20.1260.10; -; 1.
DR   InterPro; IPR001519; Ferritin.
DR   InterPro; IPR012347; Ferritin-like.
DR   InterPro; IPR009040; Ferritin-like_diiron.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR008331; Ferritin_DPS_dom.
DR   InterPro; IPR041719; Ferritin_prok.
DR   PANTHER; PTHR11431; PTHR11431; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Iron; Iron storage; Metal-binding; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..181
FT                   /note="Ferritin BfrB"
FT                   /id="PRO_0000427141"
FT   DOMAIN          5..150
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         22
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         55
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         55
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         58
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         99
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         132
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   181 AA;  20442 MW;  C0F375669A292F55 CRC64;
     MTEYEGPKTK FHALMQEQIH NEFTAAQQYV AIAVYFDSED LPQLAKHFYS QAVEERNHAM
     MLVQHLLDRD LRVEIPGVDT VRNQFDRPRE ALALALDQER TVTDQVGRLT AVARDEGDFL
     GEQFMQWFLQ EQIEEVALMA TLVRVADRAG ANLFELENFV AREVDVAPAA SGAPHAAGGR
     L