ID   FTN_BACF6               Reviewed;         159 AA.
AC   E1WS50; P28733; Q9AEU4;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Bacterial non-heme ferritin;
DE            EC=1.16.3.2;
GN   Name=ftnA; OrderedLocusNames=BF638R_2891;
OS   Bacteroides fragilis (strain 638R).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=862962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TRANSCRIPTIONAL REGULATION.
RC   STRAIN=638R;
RX   PubMed=15256555; DOI=10.1099/mic.0.26948-0;
RA   Rocha E.R., Smith C.J.;
RT   "Transcriptional regulation of the Bacteroides fragilis ferritin gene
RT   (ftnA) by redox stress.";
RL   Microbiology 150:2125-2134(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638R;
RX   PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA   Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA   Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA   Barron A., Clark L., Bentley S.D., Parkhill J.;
RT   "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT   strain capsule diversity in three strains of Bacteroides fragilis.";
RL   Microbiology 156:3255-3269(2010).
CC   -!- FUNCTION: May alleviate iron toxicity in the presence of oxygen.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide;
CC         Xref=Rhea:RHEA:11972, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:78619; EC=1.16.3.2;
CC   -!- SUBUNIT: Homooligomer of 24 subunits that assemble into a spherical
CC       protein shell (12 +/- 1 nM diameter) that can sequester at least 2000
CC       iron atoms. {ECO:0000250}.
CC   -!- INDUCTION: Expression is induced in the presence of excess iron in an
CC       oxidative environment but not in reduced anaerobic conditions. Is also
CC       regulated by oxyR. {ECO:0000269|PubMed:15256555}.
CC   -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY028371; AAK29742.1; -; Genomic_DNA.
DR   EMBL; FQ312004; CBW23380.1; -; Genomic_DNA.
DR   RefSeq; WP_005788812.1; NC_016776.1.
DR   AlphaFoldDB; E1WS50; -.
DR   SMR; E1WS50; -.
DR   GeneID; 66332292; -.
DR   KEGG; bfg:BF638R_2891; -.
DR   PATRIC; fig|862962.3.peg.2972; -.
DR   HOGENOM; CLU_065681_1_2_10; -.
DR   BRENDA; 1.16.3.2; 755.
DR   Proteomes; UP000008560; Chromosome.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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.
FT   CHAIN           1..159
FT                   /note="Bacterial non-heme ferritin"
FT                   /id="PRO_0000405241"
FT   DOMAIN          1..145
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         17
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         50
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         50
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         53
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         94
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="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   159 AA;  18064 MW;  3CAD5FC4984A0AB9 CRC64;
     MISEKLQNAI NEQISAEMWS SNLYLSMSFY FEREGFSGFA HWMKKQSQEE MGHAYAMADY
     IIKRGGIAKV DKIDVVPTGW GTPLEVFEHV FEHERHVSKL VDALVDIAAA EKDKATQDFL
     WGFVREQVEE EATAQGIVDK IKRAGDAGIF FIDSQLGQR
//