Campylobacter jejuni is the leading cause of food poisoning in Europe and North America. The exterior surface of this bacterium is encased by a capsular polysaccharide that is attached to a diacyl glycerol phosphate anchor via a poly-Kdo (3-deoxy-d-manno-oct-2-ulosinic acid) linker. In the HS:2 serotype of C. jejuni NCTC 11168, the repeating trisaccharide consists of d-ribose, N-acetyl-d-glucosamine, and d-glucuronate. Here, we show that the N-terminal domain of Cj1432 (residues 1-356) is responsible for the reaction of the C2 hydroxyl group from the terminal d-ribose moiety of the growing polysaccharide chain with UDP-d-glucuronate as the donor substrate. This discovery represents the first biochemical identification and functional characterization of a glycosyltransferase responsible for the polymerization of the capsular polysaccharide of C. jejuni. The product of the reaction catalyzed by the N-terminal domain of Cj1432 is the substrate for the reaction catalyzed by the C-terminal domain of Cj1438 (residues 453-776). This enzyme catalyzes amide bond formation using the C6 carboxylate of the terminal d-glucuronate moiety and (S)-serinol phosphate as substrates. It is also shown that Cj1435 catalyzes the hydrolysis of phosphate from the product catalyzed by the C-terminal domain of Cj1438. These results demonstrate that amide decoration of the d-glucuronate moiety occurs after the incorporation of this sugar into the growing polysaccharide chain.