Detail Information for IndEnz0007000103
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