ID FTN_HELPJ Reviewed; 167 AA. AC Q9ZLI1; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=Bacterial non-heme ferritin; DE EC=1.16.3.2; GN Name=ftnA; Synonyms=pfr; OrderedLocusNames=jhp_0598; OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J99 / ATCC 700824; RX PubMed=9923682; DOI=10.1038/16495; RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D., RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.; RT "Genomic sequence comparison of two unrelated isolates of the human gastric RT pathogen Helicobacter pylori."; RL Nature 397:176-180(1999). 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 -!- 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 -!- INTERACTION: CC Q9ZLI1; Q9ZLI1: ftnA; NbExp=4; IntAct=EBI-1210058, EBI-1210058; 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; AE001439; AAD06160.1; -; Genomic_DNA. DR PIR; D71914; D71914. DR RefSeq; WP_000949190.1; NZ_CP011330.1. DR PDB; 3BVE; X-ray; 1.80 A; A/B/C/D/E/F=1-167. DR PDB; 3BVF; X-ray; 1.50 A; A/B/C/D/E/F=1-167. DR PDB; 3BVI; X-ray; 2.00 A; A/B/C/D/E/F=1-167. DR PDB; 3BVK; X-ray; 1.50 A; A/B/C/D/E/F=1-167. DR PDB; 3BVL; X-ray; 1.80 A; A/B/C/D/E/F=1-167. DR PDB; 3EGM; X-ray; 2.10 A; A/B/C/D/E/F=1-167. DR PDB; 5C6F; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-167. DR PDBsum; 3BVE; -. DR PDBsum; 3BVF; -. DR PDBsum; 3BVI; -. DR PDBsum; 3BVK; -. DR PDBsum; 3BVL; -. DR PDBsum; 3EGM; -. DR PDBsum; 5C6F; -. DR AlphaFoldDB; Q9ZLI1; -. DR SASBDB; Q9ZLI1; -. DR SMR; Q9ZLI1; -. DR DIP; DIP-45565N; -. DR KEGG; hpj:jhp_0598; -. DR PATRIC; fig|85963.30.peg.387; -. DR eggNOG; COG1528; Bacteria. DR EvolutionaryTrace; Q9ZLI1; -. DR Proteomes; UP000000804; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. 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 3D-structure; Cytoplasm; Iron; Iron storage; Metal-binding; Oxidoreductase. FT CHAIN 1..167 FT /note="Bacterial non-heme ferritin" FT /id="PRO_0000201097" 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" FT HELIX 4..32 FT /evidence="ECO:0007829|PDB:3BVF" FT TURN 33..35 FT /evidence="ECO:0007829|PDB:3BVF" FT HELIX 37..63 FT /evidence="ECO:0007829|PDB:3BVF" FT HELIX 83..110 FT /evidence="ECO:0007829|PDB:3BVF" FT HELIX 114..119 FT /evidence="ECO:0007829|PDB:3BVF" FT HELIX 121..144 FT /evidence="ECO:0007829|PDB:3BVF" FT STRAND 146..149 FT /evidence="ECO:0007829|PDB:3BVF" FT HELIX 150..165 FT /evidence="ECO:0007829|PDB:3BVF" SQ SEQUENCE 167 AA; 19314 MW; D18B7F3F2CAD9CFC CRC64; MLSKDIIKLL NEQVNKEMNS SNLYMSMSSW CYTHSLDGAG LFLFDHAAEE YEHAKKLIIF LNENNVPVQL TSISAPEHKF EGLTQIFQKA YEHEQHISES INNIVDHAIK SKDHATFNFL QWYVAEQHEE EVLFKDILDK IELIGNENHG LYLADQYVKG IAKSRKS //