FTN_HELPJ
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 03-AUG-2022, entry version 123.
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; Proteobacteria; 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}.
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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 SMR; Q9ZLI1; -.
DR DIP; DIP-45565N; -.
DR STRING; 85963.jhp_0598; -.
DR EnsemblBacteria; AAD06160; AAD06160; jhp_0598.
DR KEGG; hpj:jhp_0598; -.
DR PATRIC; fig|85963.30.peg.387; -.
DR eggNOG; COG1528; Bacteria.
DR OMA; CEDKGFE; -.
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: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.
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
