ID FTN_CAMJE Reviewed; 167 AA. AC Q46106; Q0PAQ5; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 135. DE RecName: Full=Bacterial non-heme ferritin; DE EC=1.16.3.2; GN Name=ftn; Synonyms=cft; OrderedLocusNames=Cj0612c; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8809765; DOI=10.1111/j.1365-2958.1996.tb02633.x; RA Wai S., Nakayama K., Umene K., Moriya T., Amako K.; RT "Construction of a ferritin-deficient mutant of Campylobacter jejuni: RT contribution of ferritin to iron storage and protection against oxidative RT stress."; RL Mol. Microbiol. 20:1127-1134(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). CC -!- FUNCTION: Iron-storage protein. 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 -!- SUBCELLULAR LOCATION: Cytoplasm. 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; D64082; BAA10964.1; -; Genomic_DNA. DR EMBL; AL111168; CAL34758.1; -; Genomic_DNA. DR PIR; S77578; S77578. DR RefSeq; WP_002852256.1; NZ_SZUC01000002.1. DR RefSeq; YP_002344042.1; NC_002163.1. DR PDB; 1KRQ; X-ray; 2.70 A; A=1-167. DR PDBsum; 1KRQ; -. DR AlphaFoldDB; Q46106; -. DR SMR; Q46106; -. DR STRING; 192222.Cj0612c; -. DR PaxDb; 192222-Cj0612c; -. DR EnsemblBacteria; CAL34758; CAL34758; Cj0612c. DR GeneID; 904939; -. DR KEGG; cje:Cj0612c; -. DR PATRIC; fig|192222.6.peg.604; -. DR eggNOG; COG1528; Bacteria. DR HOGENOM; CLU_065681_1_0_7; -. DR OrthoDB; 9801481at2; -. DR EvolutionaryTrace; Q46106; -. DR Proteomes; UP000000799; 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Iron; Iron storage; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1..167 FT /note="Bacterial non-heme ferritin" FT /id="PRO_0000201095" 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..33 FT /evidence="ECO:0007829|PDB:1KRQ" FT HELIX 37..62 FT /evidence="ECO:0007829|PDB:1KRQ" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:1KRQ" FT HELIX 83..110 FT /evidence="ECO:0007829|PDB:1KRQ" FT HELIX 114..119 FT /evidence="ECO:0007829|PDB:1KRQ" FT HELIX 121..144 FT /evidence="ECO:0007829|PDB:1KRQ" FT TURN 147..149 FT /evidence="ECO:0007829|PDB:1KRQ" FT HELIX 150..163 FT /evidence="ECO:0007829|PDB:1KRQ" SQ SEQUENCE 167 AA; 19486 MW; B2CFB612DAD0D9DA CRC64; MLSKEVVKLL NEQINKEMYA ANLYLSMSSW CYENSLDGAG AFLFAHASEE SDHAKKLITY LNETDSHVEL QEVKQPEQNF KSLLDVFEKT YEHEQFITKS INTLVEHMLT HKDYSTFNFL QWYVSEQHEE EALFRGIVDK IKLIGEHGNG LYLADQYIKN IALSRKK //