OTU (ovarian tumor) domain of Wolbachia pipientis OTU deubiquitinase wMelOTU and similar proteins
Bacterial OTU deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12), such as Wolbachia pipientis wMelOTU, play a role in the manipulation of host ubiquitin signaling, an evolutionary strategy employed by bacterial and viral pathogens. By removing host ubiquitin signals, invading pathogens can inactivate immune response pathways and evade detection. DUBs catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. wMelOTU belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.
Jiyao W et al.(2023). "The conserved domain database in 2023.",