IED ID | IndEnz0002009947 |
Enzyme Type ID | protease009947 |
Protein Name |
Protein UmuD EC 3.4.21.- DNA polymerase V Pol V Cleaved into: Protein UmuD' |
Gene Name | umuD b1183 JW1172 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MLFIKPADLREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNQLLIQHPSATYFVKASGDSMIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITISSEDTLDVFGVVIHVVKAMR |
Enzyme Length | 139 |
Uniprot Accession Number | P0AG11 |
Absorption | |
Active Site | ACT_SITE 60; /note=For autocatalytic cleavage activity; ACT_SITE 97; /note=For autocatalytic cleavage activity |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair (PubMed:10801133). Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, called translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB) (PubMed:10801133). RecA and to a lesser extent the beta clamp-complex may target Pol V to replication complexes stalled at DNA template lesions (PubMed:10801133). {ECO:0000269|PubMed:10801133}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (10); Chain (2); Helix (3); Mutagenesis (3); Site (1) |
Keywords | 3D-structure;Autocatalytic cleavage;DNA damage;DNA repair;Hydrolase;Protease;Reference proteome;SOS mutagenesis;SOS response;Serine protease |
Interact With | Itself; P04152 |
Induction | INDUCTION: Repressed by LexA, induced by DNA damage (PubMed:10760155). Induced 1.5-fold by hydroxyurea (PubMed:20005847). {ECO:0000269|PubMed:10760155, ECO:0000269|PubMed:20005847}. |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | NMR spectroscopy (1); X-ray crystallography (2) |
Cross Reference PDB | 1AY9; 1I4V; 1UMU; |
Mapped Pubmed ID | 11483531; 16606699; 24561554; 6302271; 6311684; 8994967; |
Motif | |
Gene Encoded By | |
Mass | 15,063 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.21.B30; |