ArticleThe Journal of biological chemistry2014
The essential protein for bacterial flagella formation FlgJ functions as a β-N-acetylglucosaminidase.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 65 citations in OpenAlex.
- FlgJ cell-wall hydrolyzing activity enhances, but is not required, for flagellum assembly inJournal of bacteriology · 2026Article
- The last bacterial common ancestor encoded a complex flagellum.bioRxiv : the preprint server for biology · 2026Article
- Time-resolved transcriptomic analysis reveals envelope stress-mediated adaptation ofFrontiers in microbiology · 2026Article
- Article
- Morphogenetic penicillin-binding proteins control virulence-associated type III secretion systems inInfection and immunity · 2025Article
- An MltA-Like Lytic Transglycosylase Secreted by Bdellovibrio bacteriovorus Cleaves the Prey Septum during Predatory Invasion.Journal of bacteriology · 2023Article
- Bacteroid Development, Transcriptome, and Symbiotic Nitrogen-Fixing Comparison of Bradyrhizobium arachidis in Nodules of Peanut (Arachis hypogaea) and Medicinal Legume Sophora flavescens.Microbiology spectrum · 2023Article
- Elucidation of host and symbiont contributions to peptidoglycan metabolism based on comparative genomics of eight aphid subfamilies and their Buchnera.PLoS genetics · 2022Article
- Genomic Features of the Bundle-Forming HeliobacteriumMicroorganisms · 2022Article
- Characterization of a New Multifunctional GH20 β-Frontiers in microbiology · 2022Article
- Modulation of the Enzymatic Activity of the Flagellar Lytic Transglycosylase SltF by Rod Components and the Scaffolding Protein FlgJ inJournal of bacteriology · 2021Article
- Understanding tolerance to cell wall-active antibiotics.Annals of the New York Academy of Sciences · 2021Review
- CwlQ Is Required for Swarming Motility but Not Flagellar Assembly in Bacillus subtilis.Journal of bacteriology · 2021Article
- BB0259 Encompasses a Peptidoglycan Lytic Enzyme Function for Proper Assembly of Periplasmic Flagella inFrontiers in microbiology · 2021Article
- Living the Sweet Life: HowFoods (Basel, Switzerland) · 2020Article
- Roles of LysM and LytM domains in resuscitation-promoting factor (Rpf) activity and Rpf-mediated peptidoglycan cleavage and dormant spore reactivation.The Journal of biological chemistry · 2020Article
- Living in a Foster Home: The Single Subpolar Flagellum Fla1 ofBiomolecules · 2020Review
- Domain sliding of two Staphylococcus aureus N-acetylglucosaminidases enables their substrate-binding prior to its catalysis.Communications biology · 2020Article
- A novel bacterial β-Biotechnology for biofuels · 2020Article
- Cyclic-di-GMP Regulates Autoaggregation Through the Putative Peptidoglycan Hydrolase, EagA, and Regulates Transcription of theFrontiers in microbiology · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The flagellum is a major virulence factor of motile pathogenic bacteria. This structure requires more than 50 proteins for its biogenesis and function, one of which is FlgJ. Homologs of FlgJ produced by the β- and γ-proteobacteria, such as Salmonella enterica, Vibrio spp., and both Sphingomonas sp. and Pseudomonas spp. are bifunctional, possessing an N-terminal domain responsible for proper rod assembly and a C-terminal domain possessing peptidoglycan lytic activity. Despite the amount of research conducted on FlgJ from these and other bacteria over the past 15 years, no biochemical analysis had been conducted on any FlgJ and consequently confusion exists as to whether the enzyme is a peptidoglycan hydrolase or a lytic transglycosylase. In this study, we present the development of a novel assay for glycoside lytic enzymes and its use to provide the first enzymatic characterization of the lytic domain of FlgJ from S. enterica as the model enzyme. Surprisingly, FlgJ functions as neither a muramidase nor a lytic transglycosylases but rather as a β-N-acetylglucosaminidase. As such, FlgJ represents the first autolysin with this activity to be characterized from a Gram-negative bacterium. At its optimal pH of 4.0, the Michaelis-Menten parameters of K(m) and k(cat) for FlgJ from S. enterica were determined to be 0.64 ± 0.18 mg ml(-1) and 0.13 ± 0.016 s(-1), respectively, using purified PG as substrate. Its catalytic residues were identified as Glu(184) and Glu(223).
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