ART Database

According to Jurėnas et al. (2022): This family include the C-terminal toxic domain of the antibacterial Rhsmain protein, TreTu, which is delivered by the type VI secretion system of Salmonella enterica subsp. enterica serovar Typhimurium. This domain adopts an ADP-ribosyltransferase fold and inhibits protein synthesis by transferring an ADP-ribose group from NAD+ to the elongation factor Tu (EF-Tu). This modification is specifically placed on the side chain of the conserved D21 residue located on the P-loop of the EF-Tu G-domain. Finally, we demonstrate that the TriTu immunity protein neutralizes TreTu activity by acting like a lid that closes the catalytic site and traps the NAD+. The active site of the Salmonella toxin has an unprecedented hybrid configuration between the R-[ST]-E and H-H-h catalytic triads.

Download HMM model

Source: sequences (7ZHL_A) from: blast_nr_e=0.0001 Number of sequences: 115 Average length of the domain: 100 aa HMM: Model length: 104 Clustering level: 80% Alignment: ClustalO Additional information: sequences longer than 50 amino acids