InterPro : IPR002177

Name  DNA-binding protein Dps Short Name  DPS_DNA-bd
Type  Family Description  This group belongs to the ferritin domain superfamily and has the ferritin-like structural fold. Ferritins constitute a broad superfamily of iron storage proteins, widespread in all domains of life [, ]. Ferritins and bacterioferritins have essentially the same architecture, assembling in a 24mer cluster to form a hollow, roughly spherical, construction. This consists of a mineral core of hydrated ferric oxide and a multi-subunit protein shell, which encloses the former and assures its solubility in an aqueous environment. Due to the absence of the C-terminal fifth helix of 24mer ferritins, members of the Dps group assemble only to dodecameric protein shells [].Members of this entry were originally discovered as stress proteins, which protect DNA against oxidative stress during nutrient starvation [], hence the name Dps (DNA protection during starvation protein). Several members of the group, such as Dps from Escherichia colior the Dps homologue from Bacillus subtilis, exhibit a DNA-binding activity that is at least partially linked with iron complexation []. DNA binding by these proteins was shown to suffice for protection against oxidative DNA damage and might be mediated by magnesium ions, which bridge the protein surfaces with the polyanionic DNA [, ]. Functionally, this group is much more diverse, with many members promoting iron incorporation, while others act as immunogens, neutrophil activators [], cold-shock proteins, or constituents of fine-tangled pili []. Another mode of protection against reactive oxygen species implies the preferential consumption of hydrogen peroxide instead of oxygen during biomineralization [].For additional information please see [,].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



1 Child Features

Id Name Short Name Type
IPR023067 DNA protection during starvation protein, gammaproteobacteria Dps_gammaproteobac Family

1 Contains

Id Name Short Name Type
IPR012347 Ferritin-related Ferritin-rel Domain

0 Found In

0 Parent Features

11 Publications

First Author Title Year Journal Volume Pages
Almirón M A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. 1992 Genes Dev 6 2646-54
Bozzi M A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua. 1997 J Biol Chem 272 3259-65
Zhao G Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli. 2002 J Biol Chem 277 27689-96
Frenkiel-Krispin D Regulated phase transitions of bacterial chromatin: a non-enzymatic pathway for generic DNA protection. 2001 EMBO J 20 1184-91
Zeth K Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states. 2004 Proc Natl Acad Sci U S A 101 13780-5
Tonello F The Helicobacter pylori neutrophil-activating protein is an iron-binding protein with dodecameric structure. 1999 Mol Microbiol 34 238-46
Carrondo MA Ferritins, iron uptake and storage from the bacterioferritin viewpoint. 2003 EMBO J 22 1959-68
Wolf SG DNA protection by stress-induced biocrystallization. 1999 Nature 400 83-5
Grant RA The crystal structure of Dps, a ferritin homolog that binds and protects DNA. 1998 Nat Struct Biol 5 294-303
Brentjens RJ Fine tangled pili expressed by Haemophilus ducreyi are a novel class of pili. 1996 J Bacteriol 178 808-16
Theil EC Ferritin: at the crossroads of iron and oxygen metabolism. 2003 J Nutr 133 1549S-53S

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)