ART Database

An effector family found in Legionella. Involved in the mono-ADP-ribosylation of ubiquitin.

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 [PUBMED:27912065, PUBMED:26598703]. 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 [PUBMED:11017125, PUBMED:22524316]. 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 [PUBMED:29731171]. This specificity resides on the specific ubiquitin-binding surfaces of mART and the unique features of the PDE domain [PUBMED:29731171, PUBMED:29795346]. 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 [PUBMED:29731171, PUBMED:29795346]. 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 [PUBMED:29795346].

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Source: Pfam 34.0, rp75 Number of sequences: 11 Average length of the domain: 328 aa HMM: Model length: 338 Clustering level: 80% Alignment: ClustalO Additional information: sequences longer than 50 amino acids