Reviewed, UniProtKB/Swiss-Prot Q0P891 (DPS_CAMJE)

Names and origin

Protein names

Recommended name:
    DNA protection during starvation protein
    EC=1.16.-.-

Gene names

Name:	dps
Ordered Locus Names:	Cj1534c

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	149 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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 process	Iron storage
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular iron ion homeostasis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ferric iron binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
fliY	Q0PC74	1	EBI-1192444,EBI-1191111

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 149	149	DNA protection during starvation protein		PRO_0000253339
Sites
	Metal binding	25	1	Iron 1; shared with dodecameric partner By similarity
	Metal binding	52	1	Iron 1 By similarity
	Metal binding	56	1	Iron 1 By similarity
	Metal binding	56	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0P891-1 [UniParc]. Last modified September 19, 2006. Version 1. Checksum: 203EB8DE513D0884	FASTA	149	17,205
	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

References

	« Hide 'large scale' referencesShow '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. , 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
EMBLGenBankDDBJ	AL111168 Genomic DNA. Translation: CAL35634.1.
PIR	D81300.
RefSeq	YP_002344906.1.
3D structure databases
HSSP	HSSP built from PDB template 1JI4 based on UniProtKB P43313.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q0P891. 37 interactions.
PTM databases
PhosSite	Q0P891.
Genome annotation databases
GeneID	905816.
GenomeReviews	Gene locus Cj1534c in contig AL111168_GR.
KEGG	cje:Cj1534c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0P891.
OMA	Q0P891. LANTHHA.
Family and domain databases
InterPro	IPR002177. DPS_DNA_bd. IPR008331. Ferritin_Dps. IPR012347. Ferritin_rel. [Graphical view]
Gene3D	G3DSA:1.20.1260.10. Ferritin_rel. 1 hit.
Pfam	PF00210. Ferritin. 1 hit. [Graphical view]
PIRSF	PIRSF005900. Dps. 1 hit.
PRINTS	PR01346. HELNAPAPROT.
ProDom	PD149803. DPS. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

DPS_CAMJE

Accession

Primary (citable) accession number: Q0P891

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	September 19, 2006
Last modified:	June 16, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)