ID   FTN_HELPY               Reviewed;         167 AA.
AC   P52093;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Bacterial non-heme ferritin;
DE            EC=1.16.3.2;
GN   Name=ftnA; Synonyms=pfr; OrderedLocusNames=HP_0653;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-25.
RC   STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX   PubMed=8432720; DOI=10.1128/jb.175.4.966-972.1993;
RA   Frazier B.A., Pfeifer J.D., Russell D.G., Falk P., Olsen A.N., Hammar M.,
RA   Westblom T.U., Normark S.J.;
RT   "Paracrystalline inclusions of a novel ferritin containing nonheme iron,
RT   produced by the human gastric pathogen Helicobacter pylori: evidence for a
RT   third class of ferritins.";
RL   J. Bacteriol. 175:966-972(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-28.
RC   STRAIN=5294, ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487, and CCUG 915;
RX   PubMed=1556073; DOI=10.1128/jb.174.8.2539-2547.1992;
RA   Doig P., Austin J.W., Kostrzynska M., Trust T.J.;
RT   "Production of a conserved adhesin by the human gastroduodenal pathogen
RT   Helicobacter pylori.";
RL   J. Bacteriol. 174:2539-2547(1992).
RN   [4]
RP   CHARACTERIZATION AS A FERRITIN, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RX   PubMed=8419304; DOI=10.1128/jb.175.2.557-560.1993;
RA   Doig P., Austin J.W., Trust T.J.;
RT   "The Helicobacter pylori 19.6-kilodalton protein is an iron-containing
RT   protein resembling ferritin.";
RL   J. Bacteriol. 175:557-560(1993).
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 {ECO:0000269|PubMed:8419304}.
CC   -!- MISCELLANEOUS: Was originally thought to be an adhesin.
CC       {ECO:0000305|PubMed:1556073}.
CC   -!- MISCELLANEOUS: In PubMed:1556073 only the sequence of residues 1-12 of
CC       strain 5294 was determined.
CC   -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily.
CC       {ECO:0000305}.
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DR   EMBL; S54729; AAB25329.1; -; Genomic_DNA.
DR   EMBL; AE000511; AAD07712.1; -; Genomic_DNA.
DR   PIR; A49694; A49694.
DR   RefSeq; NP_207447.1; NC_000915.1.
DR   RefSeq; WP_000949202.1; NC_018939.1.
DR   PDB; 5U1B; X-ray; 2.81 A; A/B/C/D/E/F/G/H=1-167.
DR   PDBsum; 5U1B; -.
DR   AlphaFoldDB; P52093; -.
DR   SMR; P52093; -.
DR   DIP; DIP-3470N; -.
DR   IntAct; P52093; 6.
DR   MINT; P52093; -.
DR   STRING; 85962.C694_03375; -.
DR   PaxDb; P52093; -.
DR   EnsemblBacteria; AAD07712; AAD07712; HP_0653.
DR   KEGG; hpy:HP_0653; -.
DR   PATRIC; fig|85962.47.peg.703; -.
DR   eggNOG; COG1528; Bacteria.
DR   OMA; CEDKGFE; -.
DR   PhylomeDB; P52093; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR   GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR   GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR   GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
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; Direct protein sequencing; Iron; Iron storage;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..167
FT                   /note="Bacterial non-heme ferritin"
FT                   /id="PRO_0000201096"
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   CONFLICT        39
FT                   /note="A -> S (in Ref. 1; AAB25329)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..33
FT                   /evidence="ECO:0007829|PDB:5U1B"
FT   HELIX           37..63
FT                   /evidence="ECO:0007829|PDB:5U1B"
FT   HELIX           83..111
FT                   /evidence="ECO:0007829|PDB:5U1B"
FT   HELIX           114..144
FT                   /evidence="ECO:0007829|PDB:5U1B"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:5U1B"
FT   HELIX           150..163
FT                   /evidence="ECO:0007829|PDB:5U1B"
SQ   SEQUENCE   167 AA;  19286 MW;  2829A4EC2AE616D4 CRC64;
     MLSKDIIKLL NEQVNKEMNS SNLYMSMSSW CYTHSLDGAG LFLFDHAAEE YEHAKKLIVF
     LNENNVPVQL TSISAPEHKF EGLTQIFQKA YEHEQHISES INNIVDHAIK GKDHATFNFL
     QWYVSEQHEE EVLFKDILDK IELIGNENHG LYLADQYVKG IAKSRKS