ID   FTN_BACFR               Reviewed;         159 AA.
AC   P0CJ83; P28733; Q9AEU4;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Bacterial non-heme ferritin;
DE            EC=1.16.3.2;
GN   Name=ftnA; OrderedLocusNames=BF3048;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-30, AND SUBUNIT.
RC   STRAIN=20656-2-1;
RX   PubMed=1526453; DOI=10.1016/0378-1097(92)90430-v;
RA   Rocha E.R., Andrews S.C., Keen J.N., Brock J.H.;
RT   "Isolation of a ferritin from Bacteroides fragilis.";
RL   FEMS Microbiol. Lett. 74:207-212(1992).
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   -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP006841; BAD49794.1; -; Genomic_DNA.
DR   RefSeq; WP_005788812.1; NZ_UYXF01000004.1.
DR   RefSeq; YP_100328.1; NC_006347.1.
DR   AlphaFoldDB; P0CJ83; -.
DR   SMR; P0CJ83; -.
DR   STRING; 295405.BF3048; -.
DR   GeneID; 66332292; -.
DR   KEGG; bfr:BF3048; -.
DR   PATRIC; fig|295405.11.peg.2916; -.
DR   HOGENOM; CLU_065681_1_2_10; -.
DR   OrthoDB; 9801481at2; -.
DR   BRENDA; 1.16.3.2; 755.
DR   Proteomes; UP000002197; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..159
FT                   /note="Bacterial non-heme ferritin"
FT                   /id="PRO_0000201098"
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
//