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P0A998

- FTNA_ECOLI

UniProt

P0A998 - FTNA_ECOLI

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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

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP0A998.
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

        10         20         30         40         50
MLKPEMIEKL NEQMNLELYS SLLYQQMSAW CSYHTFEGAA AFLRRHAQEE
60 70 80 90 100
MTHMQRLFDY LTDTGNLPRI NTVESPFAEY SSLDELFQET YKHEQLITQK
110 120 130 140 150
INELAHAAMT NQDYPTFNFL QWYVSEQHEE EKLFKSIIDK LSLAGKSGEG
160
LYFIDKELST LDTQN
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.
InParanoidi P0A998.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 80 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