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Q9HMP7 (DPS_HALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 74. Feed History...

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

Names and origin

Protein namesRecommended name:
DNA protection during starvation protein
EC=1.16.-.-
Alternative name(s):
Bacterioferritin dpsA
Gene names
Name:dps
Synonyms:dpsA
Ordered Locus Names:VNG_2443G
ORF Names:OE4427R
OrganismHalobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
Taxonomic identifier64091 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium

Protein attributes

Sequence length182 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 By similarity.

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 110 Fe3+ can be deposited. Ref.4

Subcellular location

Cytoplasm By similarity.

Post-translational modification

The N-terminus is blocked.

Miscellaneous

The dps dodecamer comprises iron-binding sites for iron translocation, oxidation and nucleation. Fe2+ atoms are initially bound to the outer surface in proximity to the iron entry pore from which they are translocated toward the inter-subunit ferroxidase centers via two discrete steps. Iron oxidation proceeds by transient formation of tri-iron ferroxidase centers and Fe3+ atoms move to two distinct iron nucleation centers where iron mineralization occurs.

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 182182DNA protection during starvation protein
PRO_0000201656

Sites

Metal binding521Iron 1; shared with dodecameric partner
Metal binding791Iron 1
Metal binding831Iron 1
Metal binding831Iron 2 Potential
Site531Involved in iron translocation
Site561Involved in iron translocation
Site751Involved in iron nucleation
Site851Involved in iron translocation
Site861Involved in iron translocation
Site1541Involved in iron nucleation
Site1641Involved in iron translocation
Site1681Involved in iron translocation
Site1711Involved in iron translocation

Secondary structure

1 ................. 182
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HMP7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: BC1EA5E7C5F61636

FASTA18220,100
        10         20         30         40         50         60 
MSTQKNARAT AGEVEGSDAL RMDADRAEQC VDALNADLAN VYVLYHQLKK HHWNVEGAEF 

        70         80         90        100        110        120 
RDLHLFLGEA AETAEEVADE LAERVQALGG VPHASPETLQ AEASVDVEDE DVYDIRTSLA 

       130        140        150        160        170        180 
NDMAIYGDII EATREHTELA ENLGDHATAH MLREGLIELE DDAHHIEHYL EDDTLVTQGA 


LE

« Hide

References

« Hide 'large scale' references
[1]Oesterhelt D., Pfeiffer F.
Unpublished observations (NOV-2001)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of Halobacterium species NRC-1."
Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K. expand/collapse author list , Cruz R., Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S.
Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000) [PubMed: 11016950] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700922 / JCM 11081 / NRC-1.
[3]"The DpsA-homologue of the archaeon Halobacterium salinarum is a ferritin."
Reindel S., Anemueller S., Sawaryn A., Matzanke B.F.
Biochim. Biophys. Acta 1598:140-146(2002) [PubMed: 12147354] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-37, CIRCULAR DICHROISM ANALYSIS, PARTIAL CHARACTERIZATION.
Strain: ATCC 33171 / DSM 3754 / JCM 8978 / NCIMB 764 / NRC 34002.
[4]"Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states."
Zeth K., Offermann S., Essen L.-O., Oesterhelt D.
Proc. Natl. Acad. Sci. U.S.A. 101:13780-13785(2004) [PubMed: 15365182] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH IRON, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004437 Genomic DNA. Translation: AAG20524.1.
PIRH84394.
RefSeqNP_281044.1. NC_002607.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MOJX-ray1.90A/B/C/D1-182[»]
1TJOX-ray1.60A/B/C/D1-182[»]
1TK6X-ray2.20A/B/C/D1-182[»]
1TKOX-ray2.90A/B/C/D1-182[»]
1TKPX-ray2.20A/B/C/D1-182[»]
ProteinModelPortalQ9HMP7.
SMRQ9HMP7. Positions 2-181.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1448825.
GenomeReviewsGene locus VNG_2443G in contig AE004437_GR.
KEGGhal:VNG2443G.
NMPDRfig|64091.1.peg.2071.

Phylogenomic databases

HOGENOMHBG712946.
OMAELCCFEP.
PhylomeDBQ9HMP7.
ProtClustDBCLSK511713.

Enzyme and pathway databases

BioCycHSP64091:VNG2443G-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.
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFPIRSF005900. Dps. 1 hit.
PRINTSPR01346. HELNAPAPROT.
SUPFAMSSF47240. Ferritin/RR_like. 1 hit.
PROSITEPS00818. DPS_1. False negative.
PS00819. DPS_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPS_HALSA
AccessionPrimary (citable) accession number: Q9HMP7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: March 1, 2001
Last modified: December 14, 2011
This is version 74 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

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