v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | This entry represents death-on-curing (Doc) proteins mostly from bacteria and archaea. Bacterial toxin-antitoxin (TA) system (or "addiction module") composed of closely linked genes encoding a stable toxin that can harm the host cell and its cognate labile antitoxin, which protects the host from the toxin's deleterious effect [ ]. TA system plays a role in the adaptation of prokaryotes to stress conditions, the persistence phenomenon, programmed cell death and addiction to phages and mobile elements []. This entry includes Doc from bacteriophage P1, which forms a TA system with the prevents-host-death (Phd) protein [ , ]. It is a potent inhibitor of bacterial translation. It contains the Fido domain, also known as Fic domain, which contains a central motif conserved in most sequences (HPFx(D/E)GN(G/K)R), with the motif His contributing to Fic AMPylation (also known as adenylylation). However, Doc has been shown to be a protein kinase that inhibits bacterial translation by phosphorylating the conserved threonine (Thr-382) of the translation elongation factor EF-Tu rendering it unable to bind aminoacylated tRNAs [, ]. |
| Short Name | Doc |