Protein-arginine N-acetylglucosaminyltransferase NleB1
UniProtKB accession: B7UI21
Grouped By: Matching UniProtKB accession
Group Content:
Go to UniProtKB: B7UI21
UniProtKB description: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis (PubMed:20126447, PubMed:20485572, PubMed:22144899, PubMed:23955153, PubMed:24025841, PubMed:28138023, PubMed:28522607, PubMed:30979585). Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins FADD, TRADD, FAS, TNFRSF1A/TNFR1, TNFRSF25/DR3 and RIPK1: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling (PubMed:23955153, PubMed:24025841, PubMed:26883593, PubMed:28522607, PubMed:28860194, PubMed:30979585). Has preference for host FADD as substrate compared to other death domain-containing proteins (PubMed:28860194). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of HIF1A, thereby regulating host glucose metabolism (PubMed:30125331). Also displays intra-bacterial activity by mediating GlcNAcylation of glutathione synthetase GshB (PubMed:31974499). Catalyzes auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (PubMed:32432056). Shows a higher enzymatic activity than NleB2 (PubMed:23955153).
Group Members:
Release Date:
Structure Features
Sequence Features
Experimental Features
Organisms
Protein Domains
Function