ID FTN_STAHJ Reviewed; 166 AA. AC Q4L7K6; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=Bacterial non-heme ferritin; DE EC=1.16.3.2; GN Name=ftnA; OrderedLocusNames=SH1060; OS Staphylococcus haemolyticus (strain JCSC1435). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=279808; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC1435; RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005; RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., RA Hiramatsu K.; RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the RT extreme plasticity of its genome and the evolution of human-colonizing RT staphylococcal species."; RL J. Bacteriol. 187:7292-7308(2005). 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 -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP006716; BAE04369.1; -; Genomic_DNA. DR RefSeq; WP_011275365.1; NC_007168.1. DR AlphaFoldDB; Q4L7K6; -. DR SMR; Q4L7K6; -. DR GeneID; 58062765; -. DR KEGG; sha:SH1060; -. DR eggNOG; COG1528; Bacteria. DR HOGENOM; CLU_065681_1_2_9; -. DR OrthoDB; 9801481at2; -. DR Proteomes; UP000000543; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 3: Inferred from homology; KW Cytoplasm; Iron; Iron storage; Metal-binding; Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..166 FT /note="Bacterial non-heme ferritin" FT /id="PRO_0000298973" 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; 19591 MW; A147D8267DFCADCD CRC64; MLSKDLLEAL NDQMNHEYFA AHAYMAMAAY CDDASYEGFA NFYIQQAKEE RFHGKKIYDY INDRGEHAEF KSIPAPKTEF KSILETFKDG LAQEQDVTRR FYNLSEIAQK DKDYATISFL NWFLDEQVEE ESTFETHIDY LNRIGDDCNT LYLYEKELAA RSFDEE //