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Protein

Bacterial non-heme ferritin

Gene

ftnA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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 – 3330Combined sources
Helixi37 – 6327Combined sources
Helixi83 – 11028Combined sources
Helixi114 – 14330Combined sources
Helixi148 – 16013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP0A998.
PRIDEiP0A998.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0914.
EcoGeneiEG10921. ftnA.

Phylogenomic databases

eggNOGiCOG1528.
HOGENOMiHOG000223382.
InParanoidiP0A998.
KOiK02217.
OMAiCEDKGFE.
OrthoDBiEOG6G4W12.
PhylomeDBiP0A998.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A998.
PROiP0A998.

Gene expression databases

GenevestigatoriP0A998.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 82 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.