v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | The SidE family includes four large proteins SidE, SdeA, SdeB, and SdeC, required for efficient intracellular bacterial replication and catalyses ubiquitination in an E1/E2-independent manner. These proteins contain four domains: a DUB domain, a phosphodiesterase (PDE) domain, a mono-ADP-ribosyltransferase (mART) domain, and a coiled-coil (CC) domain [ , ].Ubiquitination is a post-translational modification that regulates many cellular processes, the conventional ubiquitination cascade culminates in a covalent linkage between the C terminus of ubiquitin (Ub) and a target protein [ , ]. SidE family proteins can catalyse the non-canonical ubiquitination of several different substrate proteins, including Rab small GTPases, Reticulon-4 (Rtn4), and Rag small GTPases, as well as SidE proteins themselves []. This specificity resides on the specific ubiquitin-binding surfaces of mART and the unique features of the PDE domain [, ].The DUB activity of SdeA is important for regulating the dynamics of ubiquitin association with the bacterial phagosome, but is not necessary for its role in intracellular bacterial replication [ , ].This entry represents the mono-ADP-ribosyltransferase (mART) domain that mediates the mono-ADP-ribosylation of ubiquitin, which is then transferred to serine residues of host proteins [ ]. |
| Short Name | SidE_mART |