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P0A998

- FTNA_ECOLI

UniProt

P0A998 - FTNA_ECOLI

Protein

Bacterial non-heme ferritin

Gene

ftnA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    Iron-storage protein.1 Publication

    Catalytic activityi

    4 Fe2+ + O2 + 6 H2O = 4 (FeO(OH)) + 8 H+.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi17 – 171Iron 1
    Metal bindingi49 – 491Iron 3
    Metal bindingi50 – 501Iron 1
    Metal bindingi50 – 501Iron 2
    Metal bindingi53 – 531Iron 1
    Metal bindingi94 – 941Iron 2
    Metal bindingi126 – 1261Iron 3
    Metal bindingi127 – 1271Iron 2
    Metal bindingi130 – 1301Iron 2
    Metal bindingi130 – 1301Iron 3

    GO - Molecular functioni

    1. ferric iron binding Source: EcoCyc
    2. ferroxidase activity Source: EcoCyc
    3. identical protein binding Source: EcoCyc

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: EcoliWiki
    2. intracellular sequestering of iron ion Source: EcoCyc
    3. iron ion transport Source: InterPro
    4. response to oxidative stress Source: CACAO

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Iron storage

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10921-MONOMER.
    ECOL316407:JW1893-MONOMER.
    MetaCyc:EG10921-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bacterial non-heme ferritin (EC:1.16.3.2)
    Alternative name(s):
    Ferritin-1
    Gene namesi
    Name:ftnA
    Synonyms:ftn, gen-165, rsgA
    Ordered Locus Names:b1905, JW1893
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10921. ftnA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi17 – 171E → A: Initially 100-fold slower Fe(2+) oxidation rate. 1 Publication
    Mutagenesisi24 – 241Y → F: Initially reduces Fe(2+)/O(2) stoichiometry from 3.1 to 2.2. 1 Publication
    Mutagenesisi49 – 491E → A: Initially reduces Fe(2+)/O(2) stoichiometry from ~3 to ~2. 1 Publication
    Mutagenesisi53 – 531H → A: Initially 6000-fold slower Fe(2+) oxidation rate. 1 Publication
    Mutagenesisi94 – 941E → A: Initially 200-fold slower Fe(2+) oxidation rate. 1 Publication
    Mutagenesisi126 – 1261E → A: Initially reduces Fe(2+)/O(2) stoichiometry from ~3 to ~2. 1 Publication
    Mutagenesisi130 – 1301E → A: Initially reduces Fe(2+)/O(2) stoichiometry from ~3 to ~2. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 165165Bacterial non-heme ferritinPRO_0000201085Add
    BLAST

    Proteomic databases

    PaxDbiP0A998.
    PRIDEiP0A998.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A998.

    Interactioni

    Subunit structurei

    Homooligomer of 24 subunits that assemble into a spherical protein shell (12 +/- 1 nM diameter) that can sequester at least 2000 iron atoms.2 Publications

    Protein-protein interaction databases

    DIPiDIP-36198N.
    IntActiP0A998. 2 interactions.
    STRINGi511145.b1905.

    Structurei

    Secondary structure

    1
    165
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 3330
    Helixi37 – 6327
    Helixi83 – 11028
    Helixi114 – 14330
    Helixi148 – 16013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EUMX-ray2.05A/B/C/D/E/F1-165[»]
    ProteinModelPortaliP0A998.
    SMRiP0A998. Positions 2-162.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A998.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 145145Ferritin-like diironPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ferritin family. Prokaryotic subfamily.Curated
    Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1528.
    HOGENOMiHOG000223382.
    KOiK02217.
    OMAiCEDKGFE.
    OrthoDBiEOG6G4W12.
    PhylomeDBiP0A998.

    Family and domain databases

    Gene3Di1.20.1260.10. 1 hit.
    InterProiIPR001519. Ferritin.
    IPR009040. Ferritin-like_diiron.
    IPR009078. Ferritin-like_SF.
    IPR012347. Ferritin-rel.
    IPR008331. Ferritin_DPS_dom.
    [Graphical view]
    PANTHERiPTHR11431. PTHR11431. 1 hit.
    PfamiPF00210. Ferritin. 1 hit.
    [Graphical view]
    SUPFAMiSSF47240. SSF47240. 1 hit.
    PROSITEiPS50905. FERRITIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A998-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKPEMIEKL NEQMNLELYS SLLYQQMSAW CSYHTFEGAA AFLRRHAQEE    50
    MTHMQRLFDY LTDTGNLPRI NTVESPFAEY SSLDELFQET YKHEQLITQK 100
    INELAHAAMT NQDYPTFNFL QWYVSEQHEE EKLFKSIIDK LSLAGKSGEG 150
    LYFIDKELST LDTQN 165
    Length:165
    Mass (Da):19,424
    Last modified:July 19, 2005 - v1
    Checksum:i5B3AA08BCFE6CDA0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53513 Genomic DNA. Translation: CAA37593.1.
    U00096 Genomic DNA. Translation: AAC74975.1.
    AP009048 Genomic DNA. Translation: BAA15728.1.
    U35066 Genomic DNA. Translation: AAA79049.1.
    PIRiS14069.
    RefSeqiNP_416418.1. NC_000913.3.
    YP_490165.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74975; AAC74975; b1905.
    BAA15728; BAA15728; BAA15728.
    GeneIDi12934013.
    946410.
    KEGGiecj:Y75_p1879.
    eco:b1905.
    PATRICi32119139. VBIEscCol129921_1987.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53513 Genomic DNA. Translation: CAA37593.1 .
    U00096 Genomic DNA. Translation: AAC74975.1 .
    AP009048 Genomic DNA. Translation: BAA15728.1 .
    U35066 Genomic DNA. Translation: AAA79049.1 .
    PIRi S14069.
    RefSeqi NP_416418.1. NC_000913.3.
    YP_490165.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EUM X-ray 2.05 A/B/C/D/E/F 1-165 [» ]
    ProteinModelPortali P0A998.
    SMRi P0A998. Positions 2-162.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36198N.
    IntActi P0A998. 2 interactions.
    STRINGi 511145.b1905.

    Proteomic databases

    PaxDbi P0A998.
    PRIDEi P0A998.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74975 ; AAC74975 ; b1905 .
    BAA15728 ; BAA15728 ; BAA15728 .
    GeneIDi 12934013.
    946410.
    KEGGi ecj:Y75_p1879.
    eco:b1905.
    PATRICi 32119139. VBIEscCol129921_1987.

    Organism-specific databases

    EchoBASEi EB0914.
    EcoGenei EG10921. ftnA.

    Phylogenomic databases

    eggNOGi COG1528.
    HOGENOMi HOG000223382.
    KOi K02217.
    OMAi CEDKGFE.
    OrthoDBi EOG6G4W12.
    PhylomeDBi P0A998.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10921-MONOMER.
    ECOL316407:JW1893-MONOMER.
    MetaCyc:EG10921-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A998.
    PROi P0A998.

    Gene expression databases

    Genevestigatori P0A998.

    Family and domain databases

    Gene3Di 1.20.1260.10. 1 hit.
    InterProi IPR001519. Ferritin.
    IPR009040. Ferritin-like_diiron.
    IPR009078. Ferritin-like_SF.
    IPR012347. Ferritin-rel.
    IPR008331. Ferritin_DPS_dom.
    [Graphical view ]
    PANTHERi PTHR11431. PTHR11431. 1 hit.
    Pfami PF00210. Ferritin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47240. SSF47240. 1 hit.
    PROSITEi PS50905. FERRITIN_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of an Escherichia coli K12 gene which encodes a polypeptide having similarity to the human ferritin H subunit."
      Izuhara M., Takamune K., Takata R.
      Mol. Gen. Genet. 225:510-513(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. Robison K., O'Keeffe T., Church G.M.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 151-165.
      Strain: K12 / EMG2.
    6. "Overproduction, purification and characterization of the Escherichia coli ferritin."
      Hudson A.J., Andrews S.C., Hawkins C., Williams J.M., Izuhara M., Meldrum F.C., Mann S., Harrison P.M., Guest J.R.
      Eur. J. Biochem. 218:985-995(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-20, SUBUNIT, IRON CONTENT, MOSSBAUER SPECTROSCOPY.
    7. "How the presence of three iron binding sites affects the iron storage function of the ferritin (EcFtnA) of Escherichia coli."
      Treffry A., Zhao Z., Quail M.A., Guest J.R., Harrison P.M.
      FEBS Lett. 432:213-218(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "Functionality of the three-site ferroxidase center of Escherichia coli bacterial ferritin (EcFtnA)."
      Bou-Abdallah F., Yang H., Awomolo A., Cooper B., Woodhall M.R., Andrews S.C., Chasteen N.D.
      Biochemistry 53:483-495(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-17; TYR-24; GLU-49; HIS-53; GLU-94; GLU-126 AND GLU-130, REACTION MECHANISM, EPR SPECTROSCOPY.
    9. "The high-resolution X-ray crystallographic structure of the ferritin (EcFtnA) of Escherichia coli; comparison with human H ferritin (HuHF) and the structures of the Fe(3+) and Zn(2+) derivatives."
      Stillman T.J., Hempstead P.D., Artymiuk P.J., Andrews S.C., Hudson A.J., Treffry A., Guest J.R., Harrison P.M.
      J. Mol. Biol. 307:587-603(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiFTNA_ECOLI
    AccessioniPrimary (citable) accession number: P0A998
    Secondary accession number(s): P23887
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3