ArticleThe Biochemical journal2016
EssC: domain structures inform on the elusive translocation channel in the Type VII secretion system.
Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed.
- Article
- Type VIIb secretion systems in Lactobacillales: insights from streptococci and enterococci.Journal of bacteriology · 2026Review
- EsxA is required for antibacterial toxin export by the type VIIb secretion system.The Journal of biological chemistry · 2026Article
- Distinct immunity protein families mediate compartment-specific neutralization of a bacterial toxin.Cell reports · 2025Article
- Adaptive Tolerance of Listeria monocytogenes to Chemical Oxidants: Comparative Analysis of Transcriptomic Studies.Comprehensive reviews in food science and food safety · 2025Review
- New insights into the domain of unknown function (DUF) of EccCActa crystallographica. Section D, Structural biology · 2024Article
- Structure of a tripartite protein complex that targets toxins to the type VII secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The role of proteinaceous toxins secreted byFEMS microbes · 2024Review
- Article
- A type VII-secreted lipase toxin with reverse domain arrangement.Nature communications · 2023Article
- Interbacterial competition mediated by the type VIIb secretion system.Microbiology (Reading, England) · 2023Review
- A novel variant of theMicrobial genomics · 2023Article
- Article
- Homologous recombination between tandem paralogues drives evolution of a subset of type VII secretion system immunity genes in firmicute bacteria.Microbial genomics · 2022Article
- A type VII secretion system in Group B Streptococcus mediates cytotoxicity and virulence.PLoS pathogens · 2021Article
- The Type VII Secretion System ofAnnual review of microbiology · 2021Article
- Type VII secretion systems: structure, functions and transport models.Nature reviews. Microbiology · 2021Review
- Extreme genetic diversity in the type VII secretion system ofMicrobiology (Reading, England) · 2021Article
- The type VII secretion system protects Staphylococcus aureus against antimicrobial host fatty acids.Scientific reports · 2020Article
- A membrane-depolarizing toxin substrate of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
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7 authors.
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Abstract
The membrane-bound protein EssC is an integral component of the bacterial Type VII secretion system (T7SS), which is a determinant of virulence in important Gram-positive pathogens. The protein is predicted to consist of an intracellular repeat of forkhead-associated (FHA) domains at the N-terminus, two transmembrane helices and three P-loop-containing ATPase-type domains, D1-D3, forming the C-terminal intracellular segment. We present crystal structures of the N-terminal FHA domains (EssC-N) and a C-terminal fragment EssC-C from Geobacillus thermodenitrificans, encompassing two of the ATPase-type modules, D2 and D3. Module D2 binds ATP with high affinity whereas D3 does not. The EssC-N and EssC-C constructs are monomeric in solution, but the full-length recombinant protein, with a molecular mass of approximately 169 kDa, forms a multimer of approximately 1 MDa. The observation of protomer contacts in the crystal structure of EssC-C together with similarity to the DNA translocase FtsK, suggests a model for a hexameric EssC assembly. Such an observation potentially identifies the key, and to date elusive, component of pore formation required for secretion by this recently discovered secretion system. The juxtaposition of the FHA domains suggests potential for interacting with other components of the secretion system. The structural data were used to guide an analysis of which domains are required for the T7SS machine to function in pathogenic Staphylococcus aureus The extreme C-terminal ATPase domain appears to be essential for EssC activity as a key part of the T7SS, whereas D2 and FHA domains are required for the production of a stable and functional protein.
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