ID   BFRB_MYCTE              Reviewed;         181 AA.
AC   H8F1Z2;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 2.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Ferritin BfrB;
DE            EC=1.16.3.1;
DE   AltName: Full=Bacterioferritin;
DE   AltName: Full=Non-heme ferritin Ftn;
DE   AltName: Full=Nox19;
GN   Name=bfrB; OrderedLocusNames=ERDMAN_4208;
OS   Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=652616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=22535945; DOI=10.1128/jb.00353-12;
RA   Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT   "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL   J. Bacteriol. 194:2770-2770(2012).
RN   [2]
RP   INDUCTION.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=20545848; DOI=10.1111/j.1365-2958.2010.07232.x;
RA   Sklar J.G., Makinoshima H., Schneider J.S., Glickman M.S.;
RT   "M. tuberculosis intramembrane protease Rip1 controls transcription through
RT   three anti-sigma factor substrates.";
RL   Mol. Microbiol. 77:605-617(2010).
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   -!- INDUCTION: Repressed by Rip1, highly induced by metal chelator
CC       phenanthroline in the absence of Rip1. {ECO:0000269|PubMed:20545848}.
CC   -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAL67972.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP012340; BAL67972.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003420920.1; NZ_KK339488.1.
DR   AlphaFoldDB; H8F1Z2; -.
DR   SMR; H8F1Z2; -.
DR   GeneID; 45427842; -.
DR   KEGG; mtn:ERDMAN_4208; -.
DR   PATRIC; fig|652616.3.peg.4283; -.
DR   HOGENOM; CLU_065681_1_1_11; -.
DR   Proteomes; UP000007568; 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:intracellular 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; FERRITIN; 1.
DR   PANTHER; PTHR11431:SF75; FERRITIN; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Iron; Iron storage; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..181
FT                   /note="Ferritin BfrB"
FT                   /id="PRO_0000422687"
FT   DOMAIN          15..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
//