IED ID | IndEnz0002000079 |
Enzyme Type ID | protease000079 |
Protein Name |
Antitoxin phd Addiction protein pdh Prevent host death protein |
Gene Name | phd |
Organism | Escherichia phage P1 (Bacteriophage P1) |
Taxonomic Lineage | Viruses Duplodnaviria Heunggongvirae Uroviricota Caudoviricetes Caudovirales Myoviridae (phages with contractile tails) Punavirus Escherichia phage P1 (Bacteriophage P1) |
Enzyme Sequence | MQSINFRTARGNLSEVLNNVEAGEEVEITRRGREPAVIVSKATFEAYKKAALDAEFASLFDTLDSTNKELVNR |
Enzyme Length | 73 |
Uniprot Accession Number | Q06253 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system (PubMed:18398006, PubMed:24141193, PubMed:18757857). A labile antitoxin that binds to cognate doc toxin and neutralizes its ability to phosphorylate host EF-Tu. Does not reverse phosphorylation. Bacteriophage P1 lysogenizes bacteria as a low-copy number plasmid; phd and doc proteins function in unison to stabilize plasmid number by inducing a lethal response to P1 plasmid prophage loss (PubMed:8411153). {ECO:0000269|PubMed:18398006, ECO:0000269|PubMed:18757857, ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8411153}.; FUNCTION: Binds to its own promoter repressing its expression; toxin doc acts as a corepressor or derepressor depending on the ratio, repressing or inducing expression. {ECO:0000269|PubMed:20603017, ECO:0000269|PubMed:9829946}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (4); Chain (1); Helix (5); Mutagenesis (3); Region (1); Turn (1) |
Keywords | 3D-structure;Reference proteome;Repressor;Toxin-antitoxin system;Transcription;Transcription regulation |
Interact With | Q06259 |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | PTM: Degraded by the ClpXP protease. {ECO:0000269|PubMed:7724551}. |
Signal Peptide | |
Structure 3D | X-ray crystallography (8) |
Cross Reference PDB | 3DD7; 3HRY; 3HS2; 3K33; 3KH2; 4ZLX; 4ZM0; 4ZM2; |
Mapped Pubmed ID | 27159580; |
Motif | |
Gene Encoded By | |
Mass | 8,133 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |