ArticleJournal of bacteriology2014
Flavobacterium johnsoniae chitinase ChiA is required for chitin utilization and is secreted by the type IX secretion system.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 104 citations in OpenAlex.
- Additional Binding Domain of Marine Chitinase Increases Binding Specificity and Prolongs the Lifetime of Productive Binding State.Biochemistry · 2026Article
- Development of a high-throughput growth assay for bacteria or yeasts using an agar-based insoluble carbon source immobilization method.Microbiology spectrum · 2026Article
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- Ugd Is Involved in the Synthesis of Glycans of Glycoprotein and LPS and Is Important for Cellulose Degradation inMicroorganisms · 2025Article
- Functional division of labor in motility, lignocellulose digestion, and nitrogen metabolism revealed for the Mixotricha paradoxa holobiont.The ISME journal · 2025Article
- Advances in the type IX secretion system: an exploration focusing onCurrent research in microbial sciences · 2025Review
- Diversity and composition of soil microbial communities in the rhizospheres of late blight-resistant tomatoes afterFrontiers in plant science · 2025Article
- Unveiling the molecular mechanisms of the type IX secretion system's response regulator: Structural and functional insights.PNAS nexus · 2024Article
- Ecological, beneficial, and pathogenic functions of the Type 9 Secretion System.Microbial biotechnology · 2024Review
- Structural and functional insights into the C-terminal signal domain of the Bacteroidetes type-IX secretion system.Open biology · 2024Article
- Structural insights into the mechanism of protein transport by the Type 9 Secretion System translocon.Nature microbiology · 2024Article
- A comprehensive comparative genomic analysis revealed that plant growth promoting traits are ubiquitous in strains ofFrontiers in microbiology · 2024Article
- α-1,3-Glucanase from the gram-negative bacterium Flavobacterium sp. EK-14 hydrolyzes fungal cell wall α-1,3-glucan.Scientific reports · 2023Article
- Enrichment Pretreatment Expands the Microbial Diversity Cultivated from Marine Sediments.Microorganisms · 2023Article
- Article
- A journey with type IX secretion system effectors: selection, transport, processing and activities.Microbiology (Reading, England) · 2023Article
- Filamentous structures in the cell envelope are associated with bacteroidetes gliding machinery.Communications biology · 2023Article
- Transposon mutagenesis and genome sequencing identify two novel, tandem genes involved in the colony spreading ofFrontiers in cellular and infection microbiology · 2023Article
- Purification, crystallization and crystallographic analysis of the PorX response regulator associated with the type IX secretion system.Acta crystallographica. Section F, Structural biology communications · 2022Article
- The type IX secretion system: Insights into its function and connection to glycosylation inEngineering microbiology · 2022Review
3 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flavobacterium johnsoniae, a member of phylum Bacteriodetes, is a gliding bacterium that digests insoluble chitin and many other polysaccharides. A novel protein secretion system, the type IX secretion system (T9SS), is required for gliding motility and for chitin utilization. Five potential chitinases were identified by genome analysis. Fjoh_4555 (ChiA), a 168.9-kDa protein with two glycoside hydrolase family 18 (GH18) domains, was targeted for analysis. Disruption of chiA by insertional mutagenesis resulted in cells that failed to digest chitin, and complementation with wild-type chiA on a plasmid restored chitin utilization. Antiserum raised against recombinant ChiA was used to detect the protein and to characterize its secretion by F. johnsoniae. ChiA was secreted in soluble form by wild-type cells but remained cell associated in strains carrying mutations in any of the T9SS genes, gldK, gldL, gldM, gldNO, sprA, sprE, and sprT. Western blot and liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses suggested that ChiA was proteolytically processed into two GH18 domain-containing proteins. Proteins secreted by T9SSs typically have conserved carboxy-terminal domains (CTDs) belonging to the TIGRFAM families TIGR04131 and TIGR04183. ChiA does not exhibit strong similarity to these sequences and instead has a novel CTD. Deletion of this CTD resulted in accumulation of ChiA inside cells. Fusion of the ChiA CTD to recombinant mCherry resulted in secretion of mCherry into the medium. The results indicate that ChiA is a soluble extracellular chitinase required for chitin utilization and that it relies on a novel CTD for secretion by the F. johnsoniae T9SS.
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