ID   FTNA_ECOLI              Reviewed;         165 AA.
AC   P0A998; P23887;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=Bacterial non-heme ferritin;
DE            EC=1.16.3.2;
DE   AltName: Full=Ferritin-1;
GN   Name=ftnA; Synonyms=ftn, gen-165, rsgA;
GN   OrderedLocusNames=b1905, JW1893;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2017145; DOI=10.1007/bf00261694;
RA   Izuhara M., Takamune K., Takata R.;
RT   "Cloning and sequencing of an Escherichia coli K12 gene which encodes a
RT   polypeptide having similarity to the human ferritin H subunit.";
RL   Mol. Gen. Genet. 225:510-513(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 151-165.
RC   STRAIN=K12 / EMG2;
RA   Robison K., O'Keeffe T., Church G.M.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 1-20, SUBUNIT, IRON CONTENT, AND MOSSBAUER
RP   SPECTROSCOPY.
RX   PubMed=8281950; DOI=10.1111/j.1432-1033.1993.tb18457.x;
RA   Hudson A.J., Andrews S.C., Hawkins C., Williams J.M., Izuhara M.,
RA   Meldrum F.C., Mann S., Harrison P.M., Guest J.R.;
RT   "Overproduction, purification and characterization of the Escherichia coli
RT   ferritin.";
RL   Eur. J. Biochem. 218:985-995(1993).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=9720927; DOI=10.1016/s0014-5793(98)00867-9;
RA   Treffry A., Zhao Z., Quail M.A., Guest J.R., Harrison P.M.;
RT   "How the presence of three iron binding sites affects the iron storage
RT   function of the ferritin (EcFtnA) of Escherichia coli.";
RL   FEBS Lett. 432:213-218(1998).
RN   [8]
RP   CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-17; TYR-24; GLU-49; HIS-53; GLU-94;
RP   GLU-126 AND GLU-130, REACTION MECHANISM, AND EPR SPECTROSCOPY.
RX   PubMed=24380371; DOI=10.1021/bi401517f;
RA   Bou-Abdallah F., Yang H., Awomolo A., Cooper B., Woodhall M.R.,
RA   Andrews S.C., Chasteen N.D.;
RT   "Functionality of the three-site ferroxidase center of Escherichia coli
RT   bacterial ferritin (EcFtnA).";
RL   Biochemistry 53:483-495(2014).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX   PubMed=11254384; DOI=10.1006/jmbi.2001.4475;
RA   Stillman T.J., Hempstead P.D., Artymiuk P.J., Andrews S.C., Hudson A.J.,
RA   Treffry A., Guest J.R., Harrison P.M.;
RT   "The high-resolution X-ray crystallographic structure of the ferritin
RT   (EcFtnA) of Escherichia coli; comparison with human H ferritin (HuHF) and
RT   the structures of the Fe(3+) and Zn(2+) derivatives.";
RL   J. Mol. Biol. 307:587-603(2001).
CC   -!- FUNCTION: Iron-storage protein. {ECO:0000269|PubMed:11254384}.
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         Evidence={ECO:0000269|PubMed:24380371};
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:0000269|PubMed:11254384, ECO:0000269|PubMed:8281950}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X53513; CAA37593.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74975.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15728.1; -; Genomic_DNA.
DR   EMBL; U35066; AAA79049.1; -; Genomic_DNA.
DR   PIR; S14069; S14069.
DR   RefSeq; NP_416418.1; NC_000913.3.
DR   RefSeq; WP_000917208.1; NZ_STEB01000026.1.
DR   PDB; 1EUM; X-ray; 2.05 A; A/B/C/D/E/F=1-165.
DR   PDB; 4XGS; X-ray; 2.25 A; A/B/C/D/E/F=2-165.
DR   PDB; 4ZTT; X-ray; 1.83 A; A/B/C/D/E/F=2-165.
DR   PDBsum; 1EUM; -.
DR   PDBsum; 4XGS; -.
DR   PDBsum; 4ZTT; -.
DR   AlphaFoldDB; P0A998; -.
DR   SMR; P0A998; -.
DR   BioGRID; 4263007; 14.
DR   DIP; DIP-36198N; -.
DR   IntAct; P0A998; 4.
DR   STRING; 511145.b1905; -.
DR   jPOST; P0A998; -.
DR   PaxDb; 511145-b1905; -.
DR   EnsemblBacteria; AAC74975; AAC74975; b1905.
DR   GeneID; 75202692; -.
DR   GeneID; 946410; -.
DR   KEGG; ecj:JW1893; -.
DR   KEGG; eco:b1905; -.
DR   PATRIC; fig|1411691.4.peg.343; -.
DR   EchoBASE; EB0914; -.
DR   eggNOG; COG1528; Bacteria.
DR   HOGENOM; CLU_065681_1_0_6; -.
DR   InParanoid; P0A998; -.
DR   OMA; CEDKGFE; -.
DR   OrthoDB; 9801481at2; -.
DR   PhylomeDB; P0A998; -.
DR   BioCyc; EcoCyc:EG10921-MONOMER; -.
DR   BioCyc; MetaCyc:EG10921-MONOMER; -.
DR   BRENDA; 1.16.3.2; 2026.
DR   EvolutionaryTrace; P0A998; -.
DR   PRO; PR:P0A998; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0008199; F:ferric iron binding; IDA:EcoCyc.
DR   GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR   GO; GO:0004322; F:ferroxidase activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0071281; P:cellular response to iron ion; IDA:CollecTF.
DR   GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   GO; GO:0006880; P:intracellular sequestering of iron ion; IMP:EcoCyc.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:CACAO.
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; Direct protein sequencing; Iron; Iron storage;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..165
FT                   /note="Bacterial non-heme ferritin"
FT                   /id="PRO_0000201085"
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   BINDING         49
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT   BINDING         50
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         50
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         53
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         126
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT   BINDING         127
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         130
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         130
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT   MUTAGEN         17
FT                   /note="E->A: Initially 100-fold slower Fe(2+) oxidation
FT                   rate."
FT                   /evidence="ECO:0000269|PubMed:24380371"
FT   MUTAGEN         24
FT                   /note="Y->F: Initially reduces Fe(2+)/O(2) stoichiometry
FT                   from 3.1 to 2.2."
FT                   /evidence="ECO:0000269|PubMed:24380371"
FT   MUTAGEN         49
FT                   /note="E->A: Initially reduces Fe(2+)/O(2) stoichiometry
FT                   from ~3 to ~2."
FT                   /evidence="ECO:0000269|PubMed:24380371"
FT   MUTAGEN         53
FT                   /note="H->A: Initially 6000-fold slower Fe(2+) oxidation
FT                   rate."
FT                   /evidence="ECO:0000269|PubMed:24380371"
FT   MUTAGEN         94
FT                   /note="E->A: Initially 200-fold slower Fe(2+) oxidation
FT                   rate."
FT                   /evidence="ECO:0000269|PubMed:24380371"
FT   MUTAGEN         126
FT                   /note="E->A: Initially reduces Fe(2+)/O(2) stoichiometry
FT                   from ~3 to ~2."
FT                   /evidence="ECO:0000269|PubMed:24380371"
FT   MUTAGEN         130
FT                   /note="E->A: Initially reduces Fe(2+)/O(2) stoichiometry
FT                   from ~3 to ~2."
FT                   /evidence="ECO:0000269|PubMed:24380371"
FT   HELIX           4..33
FT                   /evidence="ECO:0007829|PDB:4ZTT"
FT   HELIX           37..63
FT                   /evidence="ECO:0007829|PDB:4ZTT"
FT   HELIX           83..110
FT                   /evidence="ECO:0007829|PDB:4ZTT"
FT   HELIX           114..144
FT                   /evidence="ECO:0007829|PDB:4ZTT"
FT   HELIX           148..160
FT                   /evidence="ECO:0007829|PDB:4ZTT"
SQ   SEQUENCE   165 AA;  19424 MW;  5B3AA08BCFE6CDA0 CRC64;
     MLKPEMIEKL NEQMNLELYS SLLYQQMSAW CSYHTFEGAA AFLRRHAQEE MTHMQRLFDY
     LTDTGNLPRI NTVESPFAEY SSLDELFQET YKHEQLITQK INELAHAAMT NQDYPTFNFL
     QWYVSEQHEE EKLFKSIIDK LSLAGKSGEG LYFIDKELST LDTQN
//