Protein Domain : Prokaryotic ubiquitin-like protein Pup IPR008515

Type	Family
Description	This entry represents Prokaryotic ubiquitin-like protein Pup from Mycobacterium tuberculosis and similar short proteins, of 50-90 residues in length, predominantly found in Actinobacteria. Pup is covalently conjugated to the e-NH2 groups of lysines on several target proteins (pupylation) such as the malonyl CoA acyl carrier protein (FabD) [ ]. Pupylation of FabD was shown to result in its recruitment to the mycobacterial proteasome and subsequent degradation analogous to eukaryotic ubiquitin-conjugated proteins. Searches recovered Pup orthologous in all major actinobacteria lineages including the basal bifidobacteria and also sporadically in certain other bacterial lineages [].Members of this protein family, formerly known as DUF797, have a conserved motif with a G [EQ] signature at the C terminus and are suitable for conjugation via the terminal glutamate or the deamidated glutamine (as shown in the case of the Mycobacterium Pup []). Pup is structurally unrelated to the ubiquitin fold and has convergently evolved the function of protein modifier. It has a binding-induced folding recognition mechanism that is different from substrate recognition in the ubiquitin-proteasome system []. This protein, intrinsically disordered, links to target proteins via the ligase PafA, acquiring an ordered assembly to form two helices connected by a linker, positioning the C-terminal glutamate in the active site of this ligase [].
Short Name	Ubiquitin-like_Pup