Involved in the protein N-glycosylation pathway responsible for the assembly and attachment of an N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins (PubMed:18631242, PubMed:21091511, PubMed:22730124). Catalyzes the transfer of a glucuronate residue (GlcA) to a glucose residue already bound to a dolichol phosphate (DolP), a compound that serves as a glycan lipid carrier in Archaea. In vitro, is able to add GlcA to DolP-Glc in which the omega-position isoprene is not saturated. However, the likely physiological lipid substrate is alpha,omega-saturated (PubMed:28809486). an archaeal dolichyl alpha-D-glucosyl phosphate + UDP-alpha-D-glucuronate = an archaeal dolichyl beta-D-glucuronosyl-(1->4)-alpha-D-glucosyl phosphate + H(+) + UDP Cell surface structure biogenesis; S-layer biogenesis. Mutants contain only hexose-modified phosphodolichols and exhibit defective or limited motility. Belongs to the glycosyltransferase 2 family.