IED ID | IndEnz0007000103 |
Enzyme Type ID | catalase000103 |
Protein Name |
DNA protection during starvation protein EC 1.16.-.- |
Gene Name | dps pexB vtm b0812 JW0797 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MSTAKLVKSKATNLLYTRNDVSDSEKKATVELLNRQVIQFIDLSLITKQAHWNMRGANFIAVHEMLDGFRTALIDHLDTMAERAVQLGGVALGTTQVINSKTPLKSYPLDIHNVQDHLKELADRYAIVANDVRKAIGEAKDDDTADILTAASRDLDKFLWFIESNIE |
Enzyme Length | 167 |
Uniprot Accession Number | P0ABT2 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:48712, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; |
DNA Binding | |
EC Number | 1.16.-.- |
Enzyme Function | FUNCTION: During stationary phase, binds the chromosome non-specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. Dps also protects the cell from UV and gamma irradiation, iron and copper toxicity, thermal stress and acid and base shocks. Also shows a weak catalase activity. {ECO:0000269|PubMed:10403254, ECO:0000269|PubMed:1340475, ECO:0000269|PubMed:15205421, ECO:0000269|PubMed:15534364}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Helix (5); Initiator methionine (1); Metal binding (4); Sequence conflict (2); Turn (1) |
Keywords | 3D-structure;Cytoplasm;DNA condensation;DNA-binding;Direct protein sequencing;Iron;Iron storage;Metal-binding;Oxidoreductase;Reference proteome |
Interact With | P0A8Q6; P03004; Itself |
Induction | INDUCTION: Induced by RpoS and IHF in the early stationary phase. Induced by OxyR in response to oxidative stress during exponential phase. ClpXP probably directly regulate proteolysis of dps during exponential phase. ClpAP seems to play an indirect role in maintaining ongoing dps synthesis during stationary phase. {ECO:0000269|PubMed:7984106}. |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, nucleoid. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (12); Electron microscopy (1) |
Cross Reference PDB | 1DPS; 1F30; 1F33; 1JRE; 1JTS; 1L8H; 1L8I; 2W9R; 3O2H; 5XGO; 6QVX; 6ZGL; 7AQS; |
Mapped Pubmed ID | 10439394; 11230141; 15690043; 16606699; 16858726; 18284581; 19317833; 19373253; 19440203; 21777811; 28682051; 33033219; 33775657; |
Motif | |
Gene Encoded By | |
Mass | 18,695 |
Kinetics | |
Metal Binding | METAL 51; /note=Iron 1; shared with dodecameric partner; METAL 78; /note=Iron 1; METAL 82; /note=Iron 1; METAL 82; /note=Iron 2; /evidence=ECO:0000305 |
Rhea ID | RHEA:48712 |
Cross Reference Brenda |