IED ID | IndEnz0002008714 |
Enzyme Type ID | protease008714 |
Protein Name |
Repressor protein c Repc CI Gene product 1 gp1 Mu repressor MuR |
Gene Name | repc c Mup01 |
Organism | Escherichia phage Mu (Bacteriophage Mu) |
Taxonomic Lineage | Viruses Duplodnaviria Heunggongvirae Uroviricota Caudoviricetes Caudovirales Myoviridae (phages with contractile tails) Muvirus Escherichia phage Mu (Bacteriophage Mu) |
Enzyme Sequence | MKSNFIEKNNTEKSIWCSPQEIMAADGMPGSVAGVHYRANVQGWTKQKKEGVKGGKAVEYDVMSMPTKEREQVIAHLGLSTPDTGAQANEKQDSSELINKLTTTLINMIEELEPDEARKALKLLSKGGLLALMPLVFNEQKLYSFIGFSQQSIQTLMMLDALPEEKRKEILSKYGIHEQESVVVPSQEPQEVKKAV |
Enzyme Length | 196 |
Uniprot Accession Number | P06019 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Promotes latency by binding operators O1 and O2 in the enhancer/operator region, thereby repressing the transcription from the Pe (early) promoter and blocking the expression of the genes required for replication (lytic growth). Competes with DDE-recombinase A for binding to the internal activation sequence (IAS), which overlaps O1 and O2. The outcome of this competition determines if the virus enters latency or starts replication. Makes the cell immune to superinfection by repressing genes expression of any subsequent incoming viral genome. {ECO:0000269|PubMed:11517307, ECO:0000269|PubMed:12217693, ECO:0000269|PubMed:16154589, ECO:0000269|PubMed:18230617, ECO:0000269|PubMed:8626285}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (2); Chain (1); Domain (1); Erroneous initiation (3); Helix (4); Mutagenesis (3); Region (1); Turn (1) |
Keywords | 3D-structure;DNA-binding;Early protein;Host cytoplasm;Host-virus interaction;Latency-replication decision;Reference proteome;Repressor;Transcription;Transcription regulation;Viral latency;Viral latency initiation and maintenance |
Interact With | |
Induction | INDUCTION: Expressed in the early phase of the viral replicative cycle. When present at high concentration, negatively regulates its own expression by binding to O3 (PcM promoter). PcM promoter, and thus Repc expression, is blocked by Ner. The host SsrA, the ClpXP host protease that degrades Repressor c protein, the Lon protease, and the stationary phase-specific sigma factor RpoS are all influencing Mu repression in response to either temperature or stationary growth phase. Decreased availability of host SsrA in growing cells would favor latency, whereas starvation would favor Repc degradation and hence induction. {ECO:0000269|PubMed:16154589, ECO:0000269|PubMed:2524470}. |
Subcellular Location | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | PTM: C-terminally truncated forms act as exceptionally stable repressors that prevent prophage induction. |
Signal Peptide | |
Structure 3D | NMR spectroscopy (2) |
Cross Reference PDB | 1G4D; 1QPM; |
Mapped Pubmed ID | 10387082; |
Motif | |
Gene Encoded By | |
Mass | 21,822 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |