v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | Asparagine-linked glycosylation is a post-translational modification of proteins containing the conserved sequence motif Asn-X-Ser/Thr. The attachment of oligosaccharides is implicated in diverse processes such as protein folding and quality control, organism development or host-pathogen interactions. The reaction is catalysed by oligosaccharyltransferase (OST), a membrane protein complex located in the endoplasmic reticulum. The central, catalytic enzyme of OST is the STT3 subunit, which has homologues in bacteria and archaea. Structural analysis of a bacterial OST, undecaprenyl-diphosphooligosaccharide protein glycotransferase (PglB, ), revealed two domains: a transmembrane domain and a periplasmic domain. This entry represents the C-terminal periplasmic β-barrel domain [ ]. |
| Short Name | STT3_PglB_C |