Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q46106 (FTN_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferritin

EC=1.16.3.1
Gene names
Name:ftn
Synonyms:cft
Ordered Locus Names:Cj0612c
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Iron-storage protein.

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 By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the ferritin family. Prokaryotic subfamily.

Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
   Biological processIron storage
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular iron ion homeostasis

Inferred from electronic annotation. Source: UniProtKB-KW

iron ion transport

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

ferroxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 167167Ferritin
PRO_0000201095

Regions

Domain1 – 145145Ferritin-like diiron

Sites

Metal binding171Iron 1 By similarity
Metal binding501Iron 1 By similarity
Metal binding501Iron 2 By similarity
Metal binding531Iron 1 By similarity
Metal binding941Iron 2 By similarity
Metal binding1271Iron 2 By similarity

Secondary structure

............... 167
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q46106 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B2CFB612DAD0D9DA

FASTA16719,486
        10         20         30         40         50         60 
MLSKEVVKLL NEQINKEMYA ANLYLSMSSW CYENSLDGAG AFLFAHASEE SDHAKKLITY 

        70         80         90        100        110        120 
LNETDSHVEL QEVKQPEQNF KSLLDVFEKT YEHEQFITKS INTLVEHMLT HKDYSTFNFL 

       130        140        150        160 
QWYVSEQHEE EALFRGIVDK IKLIGEHGNG LYLADQYIKN IALSRKK 

« Hide

References

« Hide 'large scale' references
[1]"Construction of a ferritin-deficient mutant of Campylobacter jejuni: contribution of ferritin to iron storage and protection against oxidative stress."
Wai S., Nakayama K., Umene K., Moriya T., Amako K.
Mol. Microbiol. 20:1127-1134(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D64082 Genomic DNA. Translation: BAA10964.1.
AL111168 Genomic DNA. Translation: CAL34758.1.
PIRS77578.
RefSeqYP_002344042.1. NC_002163.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KRQX-ray2.70A1-167[»]
ProteinModelPortalQ46106.
SMRQ46106. Positions 1-164.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING192222.Cj0612c.

PTM databases

PhosSiteP0804292.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL34758; CAL34758; Cj0612c.
GeneID904939.
KEGGcje:Cj0612c.
PATRIC20058168. VBICamJej33762_0604.

Phylogenomic databases

eggNOGCOG1528.
HOGENOMHOG000223382.
KOK02217.
OMACEDKGFE.
OrthoDBEOG6G4W12.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-599-MONOMER.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERPTHR11431. PTHR11431. 1 hit.
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ46106.

Entry information

Entry nameFTN_CAMJE
AccessionPrimary (citable) accession number: Q46106
Secondary accession number(s): Q0PAQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references