PROSITE documentation PDOC00645Dps protein family signatures
Escherichia coli protein dps [1] is a DNA-binding protein, synthesized during prolonged starvation, that seems to protect DNA from oxidative damage. Dps binds DNA without any apparent sequence specificity. It is a protein of about 19 Kd that associates into a complex of 12 subunits forming two stacked hexameric rings.
Proteins similar to dps have been found in other bacteria:
- Bacillus subtilis protein mrgA.
- Antigen TpF1/TyF1 from Treponema pallidum and pertenue.
- Haemophilus ducreyi fine tangled pili major subunit (gene ftpA).
- Helicobacter pylori neutrophil-activating protein A (gene napA).
- Listeria innocua non-heme iron-containing ferritin.
- Synechococcus PCC 7942 nutrient-stress induced DNA binding protein (gene dpsA).
- A low-temperature induced protein from Anabaena variabilis.
- Haemophilus influenzae hypothetical protein HI1349.
- Synechocystis strain PCC 6803 hypothetical protein slr1894.
- A hypothetical protein encoded in the 5' region of a gene coding for a bromoperoxidase, in plasmid pOP2621 of Streptomyces aureofaciens.
All these proteins share a conserved region of about 50 residues in their central region. We have developed two signature patterns derived from both extremities of that region.
Note:There seems [2] to be a structural similarity between this family and that of eukaryotic ferritins (see <PDOC00181>).
Last update:July 1998 / Patterns and text revised.
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| 1 | Authors | Almiron M. Link A.J. Furlong D. Kolter R. |
| Title | A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. | |
| Source | Genes Dev. 6:2646-2654(1992). | |
| PubMed ID | 1340475 |
| 2 | Authors | Bozzi M. Mignogna G. Stefanini S. Barra D. Longhi C. Valenti P. Chiancone E. |
| Title | A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua. | |
| Source | J. Biol. Chem. 272:3259-3265(1997). | |
| PubMed ID | 9013563 |
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