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Significance Glycosyltransferase enzymes synthesize complex sugar-containing macromolecules that play pivotal roles in the biology of all cells. Bacteria produce a vast range of glycoconjugate structures that frequently dictate host–pathogen interactions. The composition and chain length of bacterial glycans are both important for biological function, yet the mechanisms for chain-length determination are generally poorly understood. Here, we describe a remarkable family of proteins in which each member contains multiple glycosyltransferase modules (often representing new glycosyltransferase families) for glycan polymerization and chain termination. The polymerase and terminator activities are separated by a molecular ruler that establishes product length. The modularity of these proteins provides an adaptable platform for generating antigenic diversity in nature and potential new strategies for glycoengineering.

Single polysaccharide assembly protein that integrates polymerization, termination, and chain-length quality control