FTN_CAMJE
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 03-AUG-2022, entry version 128.
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 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; 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; NC_002163.1.
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; Q46106; -.
DR PRIDE; Q46106; -.
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 OMA; CEDKGFE; -.
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: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 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
