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ECOLI:FTNA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ftnA (synonyms: ftn, gen-165, rsgA)
Protein Name(s) Bacterial non-heme ferritin

Ferritin-1

External Links
UniProt P0A998
EMBL X53513
U00096
AP009048
U35066
PIR S14069
RefSeq NP_416418.1
YP_490165.1
PDB 1EUM
PDBsum 1EUM
ProteinModelPortal P0A998
SMR P0A998
DIP DIP-36198N
IntAct P0A998
STRING 511145.b1905
PaxDb P0A998
PRIDE P0A998
EnsemblBacteria AAC74975
BAA15728
GeneID 12934013
946410
KEGG ecj:Y75_p1879
eco:b1905
PATRIC 32119139
EchoBASE EB0914
EcoGene EG10921
eggNOG COG1528
HOGENOM HOG000223382
InParanoid P0A998
KO K02217
OMA CEDKGFE
OrthoDB EOG6G4W12
PhylomeDB P0A998
BioCyc EcoCyc:EG10921-MONOMER
ECOL316407:JW1893-MONOMER
MetaCyc:EG10921-MONOMER
EvolutionaryTrace P0A998
PRO PR:P0A998
Proteomes UP000000318
UP000000625
Genevestigator P0A998
GO GO:0005829
GO:0008199
GO:0004322
GO:0042802
GO:0006974
GO:0006880
GO:0006826
GO:0006979
Gene3D 1.20.1260.10
InterPro IPR001519
IPR009040
IPR009078
IPR012347
IPR008331
PANTHER PTHR11431
Pfam PF00210
SUPFAM SSF47240
PROSITE PS50905

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0006979

iron-sulfur cluster assembly

PMID:18618270[1]

ECO:0000314

P

Fig. 3 shows that FtnA releaves the production of hydroxyl free radicals by scavenging the iron

complete
CACAO 2863

GO:0034986

iron chaperone activity

PMID:18618270[1]

ECO:0000314

F

Figure 6 shows that IscA can retrieve iron from the iron-bound FtnA.

complete

involved_in

GO:0006979

response to oxidative stress

PMID:18618270[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0071281

cellular response to iron ion

PMID:20015147[3]

ECO:0001204

in vitro transcription assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071281

cellular response to iron ion

PMID:20015147[3]

ECO:0000279

western blot evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10921
PANTHER:PTN000153092
UniProtKB:P02792
WB:WBGene00001500
WB:WBGene00001501

F

Seeded From UniProt

complete

enables

GO:0008199

ferric iron binding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10921
PANTHER:PTN000153092

F

Seeded From UniProt

complete

enables

GO:0008198

ferrous iron binding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000153092
UniProtKB:A0A0B4KHF0
UniProtKB:A0A0B4KI27

F

Seeded From UniProt

complete

involved_in

GO:0006880

intracellular sequestering of iron ion

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10921
PANTHER:PTN000153092
UniProtKB:P02794
UniProtKB:P9WNE5

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10921
EcoGene:EG13175
PANTHER:PTN000153346
UniProtKB:P9WNE5

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000153092
RGD:61813

C

Seeded From UniProt

complete

enables

GO:0005506

iron ion binding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:95588
PANTHER:PTN000153092
UniProtKB:P02792

F

Seeded From UniProt

complete

enables

GO:0004322

ferroxidase activity

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10921
PANTHER:PTN000153092
UniProtKB:P9WNE5

F

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:11967071[5]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:8281950[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008199

ferric iron binding

PMID:8281950[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006880

intracellular sequestering of iron ion

PMID:10049371[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004322

ferroxidase activity

PMID:9720927[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006826

iron ion transport

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001519

P

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001519
InterPro:IPR008331

P

Seeded From UniProt

complete

enables

GO:0008199

ferric iron binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001519
InterPro:IPR008331

F

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0409

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Bitoun, JP et al. (2008) Escherichia coli FtnA acts as an iron buffer for re-assembly of iron-sulfur clusters in response to hydrogen peroxide stress. Biometals 21 693-703 PubMed GONUTS page
  2. Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  3. 3.0 3.1 Nandal, A et al. (2010) Induction of the ferritin gene (ftnA) of Escherichia coli by Fe(2+)-Fur is mediated by reversal of H-NS silencing and is RyhB independent. Mol. Microbiol. 75 637-57 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 4.4 4.5 4.6 4.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  5. Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page
  6. 6.0 6.1 Hudson, AJ et al. (1993) Overproduction, purification and characterization of the Escherichia coli ferritin. Eur. J. Biochem. 218 985-95 PubMed GONUTS page
  7. Abdul-Tehrani, H et al. (1999) Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient. J. Bacteriol. 181 1415-28 PubMed GONUTS page
  8. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  9. Treffry, A et al. (1998) How the presence of three iron binding sites affects the iron storage function of the ferritin (EcFtnA) of Escherichia coli. FEBS Lett. 432 213-8 PubMed GONUTS page