{"doi":"10.1128/jb.00285-13","title":"Identification of a Mycoloyl Transferase Selectively Involved in O-Acylation of Polypeptides in Corynebacteriales","abstract":null,"journal":"Journal of Bacteriology","year":2013,"id":615095,"datarank":0.5495342469194471,"base_score":3.6635616461296463,"endowment":3.6635616461296463,"self_citation_contribution":0.5495342469194471,"citation_network_contribution":0.0,"self_endowment_contribution":0.5495342469194471,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":38,"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":1585197,"name":"C. de Sousa-D'Auria","orcid":null,"position":1,"is_corresponding":false},{"id":1585198,"name":"I. L. de la Sierra-Gallay","orcid":null,"position":2,"is_corresponding":false},{"id":1585199,"name":"C. Salmeron","orcid":null,"position":3,"is_corresponding":false},{"id":1585200,"name":"H. van Tilbeurgh","orcid":null,"position":4,"is_corresponding":false},{"id":1585201,"name":"N. Bayan","orcid":null,"position":5,"is_corresponding":false},{"id":1585202,"name":"C. Houssin","orcid":null,"position":6,"is_corresponding":false},{"id":1585203,"name":"M. Daffe","orcid":null,"position":7,"is_corresponding":false},{"id":1585204,"name":"M. Tropis","orcid":null,"position":8,"is_corresponding":false},{"id":1585196,"name":"E. Huc","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Identification of a Mycoloyl Transferase Selectively Involved in O-Acylation of Polypeptides in Corynebacteriales","abstract":"We have previously described the posttranslational modification of pore-forming small proteins of Corynebacterium by mycolic acid, a very-long-chain α-alkyl and β-hydroxy fatty acid. Using a combination of chemical analyses and mass spectrometry, we identified the mycoloyl transferase (Myt) that catalyzes the transfer of the fatty acid residue to yield O-acylated polypeptides. Inactivation of corynomycoloyl transferase C (cg0413 [Corynebacterium glutamicum mytC {CgmytC}]), one of the six Cgmyt genes of C. glutamicum, specifically abolished the O-modification of the pore-forming proteins PorA and PorH, which is critical for their biological activity. Expectedly, complementation of the cg0413 mutant with either the wild-type gene or its orthologues from Corynebacterium diphtheriae and Rhodococcus, but not Nocardia, fully restored the O-acylation of the porins. Consistently, the three-dimensional structure of CgMytC showed the presence of a unique loop that is absent from enzymes that transfer mycoloyl residues onto both trehalose and the cell wall arabinogalactan. These data suggest the implication of this structure in the enzyme specificity for protein instead of carbohydrate.","is_dataset_classified":null,"base_score":3.6635616461296463,"endowment":3.6635616461296463,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23852866","pmcid":"PMC3754736","openalex_id":"https://openalex.org/W2018769797","authors":[],"funders":[],"total_grants":0,"fwci":0.5504,"citation_percentile":0.6566712,"influential_citations":0,"citation_trend":[{"year":2013,"count":1},{"year":2016,"count":3},{"year":2017,"count":6},{"year":2018,"count":2},{"year":2019,"count":1},{"year":2020,"count":5},{"year":2021,"count":3},{"year":2022,"count":3},{"year":2023,"count":1},{"year":2024,"count":6},{"year":2025,"count":6},{"year":2026,"count":1}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"https://jb.asm.org/content/jb/195/18/4121.full.pdf","host_type":"journal"},{"url":"https://jb.asm.org/content/jb/195/18/4121.full.pdf","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1128/JB.00285-13","host_type":"publisher"},{"url":"https://doi.org/10.1128/jb.00285-13","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/23852866","host_type":"repository"},{"url":"http://europepmc.org/articles/PMC3754736","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3754736","host_type":"repository"}],"fields_of_study":["Microbial Metabolic Engineering and Bioproduction","Glycosylation and Glycoproteins Research","Enzyme Structure and Function"],"mesh_terms":["Acylation","Acyltransferases","Amino Acid Sequence","Bacterial Proteins","Models, Molecular","Molecular Sequence Data","Mycolic Acids","Peptides","Substrate Specificity","Porins","Corynebacterium glutamicum"],"keywords":["Corynebacterium glutamicum","Transferase","Biochemistry","Biology","Acylation","Complementation","Cell wall","Enzyme","Corynebacterium","Fatty acid","Mutant","Gene","Bacteria"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-02T18:54:24.638689Z","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":[]}