{"doi":"10.1111/mmi.13752","title":"Type IX secretion: the generation of bacterial cell surface coatings involved in virulence, gliding motility and the degradation of complex biopolymers","abstract":"<jats:title>Summary</jats:title><jats:p>The Type IX secretion system (T9SS) is present in over 1000 sequenced species/strains of the <jats:italic>Fibrobacteres‐Chlorobi‐Bacteroidetes</jats:italic> superphylum. Proteins secreted by the T9SS have an N‐terminal signal peptide for translocation across the inner membrane via the SEC translocon and a C‐terminal signal for secretion across the outer membrane via the T9SS. Nineteen protein components of the T9SS have been identified including three, SigP, PorX and PorY that are involved in regulation. The inner membrane proteins PorL and PorM and the outer membrane proteins PorK and PorN interact and a complex comprising PorK and PorN forms a large ring structure of 50 nm in diameter. PorU, PorV, PorQ and PorZ form an attachment complex on the cell surface of the oral pathogen, <jats:italic>Porphyromonas gingivalis. P. gingivalis</jats:italic> T9SS substrates bind to PorV suggesting that after translocation PorV functions as a shuttle protein to deliver T9SS substrates to the attachment complex. The PorU component of the attachment complex is a novel Gram negative sortase which catalyses the cleavage of the C‐terminal signal and conjugation of the protein substrates to lipopolysaccharide, anchoring them to the cell surface. This review presents an overview of the T9SS focusing on the function of T9SS substrates and machinery components.</jats:p>","journal":"Molecular Microbiology","year":2017,"id":659544,"datarank":0.7444266945389861,"base_score":4.962844630259907,"endowment":4.962844630259907,"self_citation_contribution":0.7444266945389861,"citation_network_contribution":0.0,"self_endowment_contribution":0.7444266945389861,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":142,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1721705,"name":"Michelle D. Glew","orcid":null,"position":1,"is_corresponding":false},{"id":1721706,"name":"Dhana G. Gorasia","orcid":null,"position":2,"is_corresponding":false},{"id":486213,"name":"Eric C. Reynolds","orcid":"0000-0002-6618-4856","position":3,"is_corresponding":false},{"id":553773,"name":"Paul D. Veith","orcid":"0000-0002-7344-1662","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Type IX secretion: the generation of bacterial cell surface coatings involved in virulence, gliding motility and the degradation of complex biopolymers","abstract":"<jats:title>Summary</jats:title><jats:p>The Type IX secretion system (T9SS) is present in over 1000 sequenced species/strains of the <jats:italic>Fibrobacteres‐Chlorobi‐Bacteroidetes</jats:italic> superphylum. Proteins secreted by the T9SS have an N‐terminal signal peptide for translocation across the inner membrane via the SEC translocon and a C‐terminal signal for secretion across the outer membrane via the T9SS. Nineteen protein components of the T9SS have been identified including three, SigP, PorX and PorY that are involved in regulation. The inner membrane proteins PorL and PorM and the outer membrane proteins PorK and PorN interact and a complex comprising PorK and PorN forms a large ring structure of 50 nm in diameter. PorU, PorV, PorQ and PorZ form an attachment complex on the cell surface of the oral pathogen, <jats:italic>Porphyromonas gingivalis. P. gingivalis</jats:italic> T9SS substrates bind to PorV suggesting that after translocation PorV functions as a shuttle protein to deliver T9SS substrates to the attachment complex. The PorU component of the attachment complex is a novel Gram negative sortase which catalyses the cleavage of the C‐terminal signal and conjugation of the protein substrates to lipopolysaccharide, anchoring them to the cell surface. This review presents an overview of the T9SS focusing on the function of T9SS substrates and machinery components.</jats:p>","is_dataset_classified":null,"base_score":4.962844630259907,"endowment":4.962844630259907,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"28714554","pmcid":null,"openalex_id":"https://openalex.org/W2736180350","authors":[],"funders":[{"funder_name":"Australian Government, Department of Industry, Innovation and Science","grant_id":"","title":null}],"total_grants":1,"fwci":14.1114,"citation_percentile":0.99152698,"influential_citations":0,"citation_trend":[{"year":2017,"count":2},{"year":2018,"count":13},{"year":2019,"count":17},{"year":2020,"count":27},{"year":2021,"count":16},{"year":2022,"count":23},{"year":2023,"count":15},{"year":2024,"count":10},{"year":2025,"count":16},{"year":2026,"count":3}],"oa_status":"green","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"http://hdl.handle.net/11343/208056","host_type":"repository"},{"url":"http://hdl.handle.net/11343/208056","host_type":"repository"},{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fmmi.13752","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/pdf/10.1111/mmi.13752","host_type":"publisher"},{"url":"https://doi.org/10.1111/mmi.13752","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/28714554","host_type":"repository"}],"fields_of_study":["Streptococcal Infections and Treatments","Neonatal and Maternal Infections","Oral microbiology and periodontitis research","Amino Acid Sequence","Bacterial Proteins","Bacterial Secretion Systems","Biopolymers","Cell Movement","Conserved Sequence","Membrane Proteins","Porphyromonas gingivalis","Protein Sorting Signals","Protein Transport","Proteolysis","Virulence"],"mesh_terms":["Amino Acid Sequence","Bacterial Proteins","Biopolymers","Cell Movement","Membrane Proteins","Virulence","Porphyromonas gingivalis","Conserved Sequence","Protein Transport","Protein Sorting Signals","Bacterial Secretion Systems","Proteolysis"],"keywords":["Porphyromonas gingivalis","Bacterial outer membrane","Secretion","Biology","Cell biology","Signal peptide","Sortase","Periplasmic space","Transport protein","Virulence","Membrane protein","Inner membrane","Peptide sequence","Biochemistry","Bacteria","Membrane","Gene","Genetics","Escherichia coli","Bacterial protein"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-12T07:07:38.662759Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}