FTNA_ECOLI
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 03-AUG-2022, entry version 125.
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; OrderedLocusNames=b1905, JW1893;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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; P0A998; -.
DR PRIDE; P0A998; -.
DR EnsemblBacteria; AAC74975; AAC74975; b1905.
DR EnsemblBacteria; BAA15728; BAA15728; BAA15728.
DR GeneID; 66674206; -.
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 PhylomeDB; P0A998; -.
DR BioCyc; EcoCyc:EG10921-MON; -.
DR BioCyc; MetaCyc:EG10921-MON; -.
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:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0071281; P:cellular response to iron ion; IDA:CollecTF.
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; 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..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
