| IED ID | IndEnz0002010419 |
| Enzyme Type ID | protease010419 |
| Protein Name |
Repressor c protein Repc CI |
| Gene Name | repc c |
| Organism | Escherichia phage D108 (Bacteriophage D108) |
| Taxonomic Lineage | Viruses Duplodnaviria Heunggongvirae Uroviricota Caudoviricetes Caudovirales Myoviridae (phages with contractile tails) Muvirus unclassified Muvirus Escherichia phage D108 (Bacteriophage D108) |
| Enzyme Sequence | MMSFEIKEWFNAKELEGMPGVPKLATNITRKAVAEDWVKRQRHGGKGVAYEYHINSLPEETRRAIKGASLSDKPVHTSIVHTVDERLIYAMSFLTPDEQAAAVEIIRVAGIKGLMPTIVSKDKALEALGITVEQQKTLQTLQALPPEKVREILSQYEGKEHNFPVRENDVKKAV |
| Enzyme Length | 174 |
| Uniprot Accession Number | P07040 |
| 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 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Region (1); Sequence conflict (1) |
| Keywords | DNA-binding;Early protein;Host cytoplasm;Host-virus interaction;Latency-replication decision;Reference proteome;Repressor;Transcription;Transcription regulation |
| 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 Repc, the Lon protease, and the stationary phase-specific sigma factor RpoS are all influencing viral 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. |
| Subcellular Location | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 19,518 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |