2.1.1.294	evolution	WarA and WarB have structural similarities with the bi-functional Escherichia coli LPS O antigen regulator WbdD. A predicted three-dimensional model is generated with a very high confidence on the Escherichia coli serotype O9a WbdD protein (19% sequence identity, 69% sequence coverage, 100% confidence)	-, 757781	
2.1.1.294	malfunction	construction of a chromosomal wbdDO9a::aacC1 mutation by allelic exchange. Membranes of the mutant are still able to synthesize O9a polymannan in vitro, although the chain length is increased relative to that made by the parent	-, 722640	
2.1.1.294	malfunction	membrane preparations from a wbdD mutant have severely diminished mannosyltransferase activity in vitro, and no significant amounts of the WbdA protein are targeted to the membrane fraction. Expression of a polypeptide comprising the WbdD C-terminal region is sufficient to restore both proper localization of WbdA and mannosyltransferase activity	-, 722664	
2.1.1.294	malfunction	The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. A phenotype of significantly increased neutrophil recruitment is observed for a warA deletion mutant. Infection with a warA mutant also induces TNF-alpha mRNA levels significantly higher than wild-type infected larvae	-, 757781	
2.1.1.294	metabolism	the enzyme WbdD takes part in the biosynthesis of lipopolysaccharide O-antigen in Escherichia coli strain O9a, genetic organization, LPS structure, and pathway, overview. Model for export of lipopolysaccharide (LPS) O-antigen polysaccharide (O-PS) via ABC transporters. In O9a biosynthesis, the chain-terminator enzyme WbdD caps the nonreducing end of the glycan with a methylphosphate moiety and thereby establishes chain-length distribution. A carbohydrate-binding module (CBM) in the ABC transporter recognizes terminated glycans, ensuring that only mature O-PS is exported and incorporated into LPS. Each CBM can bind the O-PS only with the native repeat unit, revealing that methylphosphate is essential but not sufficient for substrate recognition and export	-, 757222	
2.1.1.294	metabolism	the enzyme WbdD takes part in the biosynthesis of lipopolysaccharide O-antigen in Klebsiella pneumoniae strain O7, pathway overview	-, 757222	
2.1.1.294	additional information	direct interaction between the CBM and the terminal methyl group. The nonreducing terminal modification is the sole contributor to ABC transporter WztO9a-C O-PS recognition	-, 757222	
2.1.1.294	additional information	WarA is a methyltransferase in complex with a putative kinase WarB. WarA binds to cyclic-di-GMP, which potentiates its methyltransferase activity. Bacterial two-hybrid assay	-, 757781	
2.1.1.294	physiological function	In Escherichia coli O9a, the peripheral membrane protein WbdD terminates polymerization by adding a methyl phosphate to the non-reducing end of the nascent O9a polymer. The O9a system is a representative of the widespread ATP-binding cassette transporter-dependent assembly pathway. This terminal modification is required for recognition and export of the completed O-PS across the cytoplasmic membrane by its cognate ATP-binding cassette transporter. The recognition event is mediated by the nucleotide-binding domain polypeptide of the transporter, which possesses a serotype-specific carbohydrate-binding module that only binds terminated O-PS chains. The WbdD terminator plays an additional pivotal structural role in recruiting WbdA to the membrane. The stoichiometry of WbdA:WbdD in active complexes is a critical factor in establishing the chain length distribution of the resulting glycans. The size of the O9a polysaccharide is determined by the chain-terminating dual kinase/methyltransferase (WbdD) that is tethered to the membrane and recruits polymerase/glycosyltransferase WbdA into an active enzyme complex by protein-protein interactions. Identification via bacterial two-hybrid analysis of a surface-exposed alpha-helix in the C-terminal mannosyltransferase domain of WbdA as the site of interaction with WbdD, the C-terminal domain was unable to interact with WbdD in the absence of its N-terminal partner. The WbdD protein orchestrates critical localization and coordination of activities involved in chain extension and termination. Complex domain interactions are needed to position the polymerase components appropriately for assembly into a functional complex located at the cytoplasmic membrane. WbdD is therefore a central player in a sophisticated quality control system that dictates the distribution of chain lengths and marks those chains with a terminal export tag	736468	
2.1.1.294	physiological function	the enzyme WbdD takes part in the biosynthesis of lipopolysaccharide O-antigen in Klebsiella pneumoniae strain O7, pathway overview. In the simpler process exhibited by Klebsiella pneumoniae serotype O2a, the O-PS is polymerized to completion within the cytosol by a biosynthetic enzyme complex. The chain-length distribution is controlled by the relative activities of a complex of glycosyltransferase (GT) enzymes and the ABC transporter. The O2a ABC transporter does not possess strict O-PS specificity, and it can export polymers with diverse repeat-unit structures, but polymerization and export are obligatorily coupled	-, 757222