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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)DescriptionActionsGraphical viewLength
Metal bindingi17Iron 11
Metal bindingi49Iron 31
Metal bindingi50Iron 11
Metal bindingi50Iron 21
Metal bindingi53Iron 11
Metal bindingi94Iron 21
Metal bindingi126Iron 31
Metal bindingi127Iron 21
Metal bindingi130Iron 21
Metal bindingi130Iron 31

GO - Molecular functioni

  • ferric iron binding Source: EcoCyc
  • ferroxidase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • intracellular sequestering of iron ion Source: EcoCyc
  • iron ion transport Source: InterPro
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10921. ftnA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi17E → A: Initially 100-fold slower Fe(2+) oxidation rate. 1 Publication1
Mutagenesisi24Y → F: Initially reduces Fe(2+)/O(2) stoichiometry from 3.1 to 2.2. 1 Publication1
Mutagenesisi49E → A: Initially reduces Fe(2+)/O(2) stoichiometry from ~3 to ~2. 1 Publication1
Mutagenesisi53H → A: Initially 6000-fold slower Fe(2+) oxidation rate. 1 Publication1
Mutagenesisi94E → A: Initially 200-fold slower Fe(2+) oxidation rate. 1 Publication1
Mutagenesisi126E → A: Initially reduces Fe(2+)/O(2) stoichiometry from ~3 to ~2. 1 Publication1
Mutagenesisi130E → A: Initially reduces Fe(2+)/O(2) stoichiometry from ~3 to ~2. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002010851 – 165Bacterial non-heme ferritinAdd BLAST165

Proteomic databases

EPDiP0A998.
PaxDbiP0A998.
PRIDEiP0A998.

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

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4263007. 5 interactors.
DIPiDIP-36198N.
IntActiP0A998. 2 interactors.
STRINGi511145.b1905.

Structurei

Secondary structure

1165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 33Combined sources30
Helixi37 – 63Combined sources27
Helixi83 – 110Combined sources28
Helixi114 – 144Combined sources31
Helixi148 – 160Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EUMX-ray2.05A/B/C/D/E/F1-165[»]
4XGSX-ray2.25A/B/C/D/E/F2-165[»]
4ZTTX-ray1.83A/B/C/D/E/F2-165[»]
ProteinModelPortaliP0A998.
SMRiP0A998.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A998.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 145Ferritin-like diironPROSITE-ProRule annotationAdd BLAST145

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG41090A1. Bacteria.
COG1528. LUCA.
HOGENOMiHOG000223382.
InParanoidiP0A998.
KOiK02217.
OMAiCEDKGFE.
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.
WP_000917208.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74975; AAC74975; b1905.
BAA15728; BAA15728; BAA15728.
GeneIDi946410.
KEGGiecj:JW1893.
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.
WP_000917208.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EUMX-ray2.05A/B/C/D/E/F1-165[»]
4XGSX-ray2.25A/B/C/D/E/F2-165[»]
4ZTTX-ray1.83A/B/C/D/E/F2-165[»]
ProteinModelPortaliP0A998.
SMRiP0A998.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263007. 5 interactors.
DIPiDIP-36198N.
IntActiP0A998. 2 interactors.
STRINGi511145.b1905.

Proteomic databases

EPDiP0A998.
PaxDbiP0A998.
PRIDEiP0A998.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74975; AAC74975; b1905.
BAA15728; BAA15728; BAA15728.
GeneIDi946410.
KEGGiecj:JW1893.
eco:b1905.
PATRICi32119139. VBIEscCol129921_1987.

Organism-specific databases

EchoBASEiEB0914.
EcoGeneiEG10921. ftnA.

Phylogenomic databases

eggNOGiENOG41090A1. Bacteria.
COG1528. LUCA.
HOGENOMiHOG000223382.
InParanoidiP0A998.
KOiK02217.
OMAiCEDKGFE.
PhylomeDBiP0A998.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A998.
PROiP0A998.

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...

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: November 2, 2016
This is version 93 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

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 one 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.