Ferritin-1 - Escherichia coli (strain K12)

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P0A998 (FTNA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ferritin-1
EC=1.16.3.1

Gene names

Name:	ftnA
Synonyms:	ftn, gen-165, rsgA
Ordered Locus Names:	b1905, JW1893

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Iron-storage protein. Ref.8
Catalytic activity	4 Fe²⁺ + 4 H⁺ + O₂ = 4 Fe³⁺ + 2 H₂O.
Subunit structure	Homooligomer of 24 subunits that assemble into a spherical protein shell (12 +/- 1 nM diameter) that can sequester at least 2000 iron atoms. Ref.8
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the ferritin family. Prokaryotic subfamily. Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
Biological process	Iron storage
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intracellular sequestering of iron ion Inferred from mutant phenotype PubMed 10049371. Source: EcoCyc iron ion transport Inferred from electronic annotation. Source: InterPro response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	ferric iron binding Inferred from direct assay Ref.6. Source: EcoCyc ferroxidase activity Inferred from direct assay Ref.7. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 165

165

Ferritin-1

PRO_0000201085

Regions

Domain

1 – 145

145

Ferritin-like diiron

Sites

Metal binding

Iron 1

Metal binding

Iron 3

Metal binding

Iron 1

Metal binding

Iron 2

Metal binding

Iron 1

Metal binding

Iron 2

Metal binding

126

Iron 3

Metal binding

127

Iron 2

Metal binding

130

Iron 2

Metal binding

130

Iron 3

Secondary structure

165

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A998 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 5B3AA08BCFE6CDA0
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FASTA

165

19,424

        10         20         30         40         50         60 
MLKPEMIEKL NEQMNLELYS SLLYQQMSAW CSYHTFEGAA AFLRRHAQEE MTHMQRLFDY 

        70         80         90        100        110        120 
LTDTGNLPRI NTVESPFAEY SSLDELFQET YKHEQLITQK INELAHAAMT NQDYPTFNFL 

       130        140        150        160 
QWYVSEQHEE EKLFKSIIDK LSLAGKSGEG LYFIDKELST LDTQN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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, CHARACTERIZATION.
[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]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53513 Genomic DNA. Translation: CAA37593.1.
U00096 Genomic DNA. Translation: AAC74975.1.
AP009048 Genomic DNA. Translation: BAA15728.1.
U35066 Genomic DNA. Translation: AAA79049.1.

PIR

S14069.

RefSeq

NP_416418.1. NC_000913.2.
YP_490165.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EUM	X-ray	2.05	A/B/C/D/E/F	1-165	[»]

ProteinModelPortal

P0A998.

SMR

P0A998. Positions 2-162.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36198N.

IntAct

P0A998. 2 interactions.

STRING

511145.b1905.

Proteomic databases

PaxDb

P0A998.

PRIDE

P0A998.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74975; AAC74975; b1905.
BAA15728; BAA15728; BAA15728.

GeneID

12934013.
946410.

KEGG

ecj:Y75_p1879.
eco:b1905.

PATRIC

32119139. VBIEscCol129921_1987.

Organism-specific databases

EchoBASE

EB0914.

EcoGene

EG10921. ftnA.

Phylogenomic databases

eggNOG

COG1528.

HOGENOM

HOG000223382.

K02217.

OMA

CEDKGFE.

ProtClustDB

PRK10304.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0A998.

Family and domain databases

Gene3D

1.20.1260.10. 1 hit.

InterPro

IPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]

PANTHER

PTHR11431. PTHR11431. 1 hit.

Pfam

PF00210. Ferritin. 1 hit.
[Graphical view]

SUPFAM

SSF47240. Ferritin/RR_like. 1 hit.

PROSITE

PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A998.

Entry information

Entry name

FTNA_ECOLI

Accession

Primary (citable) accession number: P0A998
Secondary accession number(s): P23887

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents