FTN_BACFR
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 03-AUG-2022, entry version 46.
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; Bacteroidetes; 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 EnsemblBacteria; BAD49794; BAD49794; BF3048.
DR GeneID; 66332292; -.
DR KEGG; bfr:BF3048; -.
DR PATRIC; fig|295405.11.peg.2916; -.
DR HOGENOM; CLU_065681_1_2_10; -.
DR OMA; CEDKGFE; -.
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: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 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
