FTN_STAA8
ID FTN_STAA8 Reviewed; 166 AA.
AC Q2FWZ8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Bacterial non-heme ferritin;
DE EC=1.16.3.2;
GN Name=ftnA; OrderedLocusNames=SAOUHSC_02108;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP PROTEIN SEQUENCE OF 2-10, AND REGULATION BY PERR.
RX PubMed=11349039; DOI=10.1128/iai.69.6.3744-3754.2001;
RA Horsburgh M.J., Clements M.O., Crossley H., Ingham E., Foster S.J.;
RT "PerR controls oxidative stress resistance and iron storage proteins and is
RT required for virulence in Staphylococcus aureus.";
RL Infect. Immun. 69:3744-3754(2001).
RN [3]
RP INDUCTION BY IRON, AND REGULATION BY PERR AND FUR.
RX PubMed=14742543; DOI=10.1128/iai.72.2.972-979.2004;
RA Morrissey J.A., Cockayne A., Brummell K., Williams P.;
RT "The staphylococcal ferritins are differentially regulated in response to
RT iron and manganese and via perR and fur.";
RL Infect. Immun. 72:972-979(2004).
CC -!- FUNCTION: Iron-storage protein. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Induced by iron. Repressed by PerR. Negatively regulated by
CC Fur. In addition, is regulated in a PerR-independent way under metal-
CC depleted conditions. {ECO:0000269|PubMed:14742543}.
CC -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD31158.1; -; Genomic_DNA.
DR RefSeq; WP_000949467.1; NZ_LS483365.1.
DR RefSeq; YP_500600.1; NC_007795.1.
DR AlphaFoldDB; Q2FWZ8; -.
DR SMR; Q2FWZ8; -.
DR STRING; 1280.SAXN108_1991; -.
DR EnsemblBacteria; ABD31158; ABD31158; SAOUHSC_02108.
DR GeneID; 3921180; -.
DR KEGG; sao:SAOUHSC_02108; -.
DR PATRIC; fig|93061.5.peg.1913; -.
DR eggNOG; COG1528; Bacteria.
DR HOGENOM; CLU_065681_1_2_9; -.
DR OMA; CEDKGFE; -.
DR PRO; PR:Q2FWZ8; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
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 Cytoplasm; Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11349039"
FT CHAIN 2..166
FT /note="Bacterial non-heme ferritin"
FT /id="PRO_0000295894"
FT DOMAIN 2..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 166 AA; 19589 MW; A8B3B5ECFBA82EEF CRC64;
MLSKNLLEAL NDQMNHEYFA AHAYMAMAAY CDKESYEGFA NFFIQQAKEE RFHGQKIYNY
INDRGAHAEF RAVSAPKIDF SSILETFKDS LSQEQEVTRR FYNLSEIARQ DKDYATISFL
NWFLDEQVEE ESMFETHINY LTRIGDDSNA LYLYEKELGA RTFDEE
