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Q0P891 (DPS_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
DNA protection during starvation protein

EC=1.16.-.-
Gene names
Name:dps
Ordered Locus Names:Cj1534c
OrganismCampylobacter jejuni
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, which prevents hydroxyl radical production by the Fenton reaction Probable. Does not bind DNA. Ref.1

Catalytic activity

2 Fe2+ + H2O2 + 2 H+ = 2 Fe3+ + 2 H2O.

Subunit structure

Homododecamer. The 12 subunits form a hollow sphere into which the mineral iron core of up to 500 Fe3+ can be deposited By similarity.

Subcellular location

Cytoplasm By similarity.

Induction

Constitutively expressed. Not induced by hydrogen peroxide or by iron.

Sequence similarities

Belongs to the dps family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

response to stress

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

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

fliYQ0PC741EBI-1192444,EBI-1191111

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 149149DNA protection during starvation protein
PRO_0000253339

Sites

Metal binding251Iron 1; shared with dodecameric partner By similarity
Metal binding521Iron 1 By similarity
Metal binding561Iron 1 By similarity
Metal binding561Iron 2 By similarity

Secondary structure

........... 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q0P891 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: 203EB8DE513D0884

FASTA14917,205
        10         20         30         40         50         60 
MSVTKQLLQM QADAHHLWVK FHNYHWNVKG LQFFSIHEYT EKAYEEMAEL FDSCAERVLQ 

        70         80         90        100        110        120 
LGEKAITCQK VLMENAKSPK VAKDCFTPLE VIELIKQDYE YLLAEFKKLN EAAEKESDTT 

       130        140 
TAAFAQENIA KYEKSLWMIG ATLQGACKM 

« Hide

References

« Hide 'large scale' references
[1]"The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni."
Ishikawa T., Mizunoe Y., Kawabata S., Takade A., Harada M., Wai S.N., Yoshida S.
J. Bacteriol. 185:1010-1017(2003) [PubMed: 12533477] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, IRON BINDING, FUNCTION IN PROTECTION OF DNA FROM HYDROGEN PEROXIDE STRESS.
[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: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL35634.1.
PIRD81300.
RefSeqYP_002344906.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KWOX-ray1.98A/B/C/D1-149[»]
ProteinModelPortalQ0P891.
ModBaseSearch...

Protein-protein interaction databases

IntActQ0P891. 37 interactions.

PTM databases

PhosSiteQ0P891.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID905816.
GenomeReviewsGene locus Cj1534c in contig AL111168_GR.
KEGGcje:Cj1534c.
PATRIC20060028. VBICamJej33762_1511.

Phylogenomic databases

HOGENOMHBG672882.
OMANESAEQM.
PhylomeDBQ0P891.
ProtClustDBCLSK2767721.

Enzyme and pathway databases

BioCycCJEJ192222:CJ1534C-MONOMER.

Family and domain databases

InterProIPR002177. DPS_DNA-bd.
IPR012347. Ferritin-rel.
IPR009078. Ferritin/RR-like.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
Gene3DG3DSA:1.20.1260.10. Ferritin_rel. 1 hit.
KOK04047.
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFPIRSF005900. Dps. 1 hit.
PRINTSPR01346. HELNAPAPROT.
SUPFAMSSF47240. Ferritin/RR_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDPS_CAMJE
AccessionPrimary (citable) accession number: Q0P891
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: September 19, 2006
Last modified: January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families