Detail Information for IndEnz0002009947
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;