<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Moreira R</submitter><funding>Natural Sciences and Engineering Research Council of Canada</funding><funding>National Institute of Allergy and Infectious Diseases</funding><funding>NCRR NIH HHS</funding><funding>NIAID NIH HHS</funding><funding>National Institutes of Health</funding><funding>NIGMS NIH HHS</funding><pubmed_abstract>Here we describe bibacillin 1 - a two-component lantibiotic from &lt;i>Bacillus thuringiensis&lt;/i>. The peptides that comprise bibacillin 1 are modified by a class II lanthipeptide synthetase Bib1M producing two peptides with non-overlapping ring patterns that are reminiscent of cerecidin and the short component of the enterococcal cytolysin (CylL&lt;sub>S&lt;/sub>''), a virulence factor associated with human disease. Stereochemical analysis demonstrated that each component contains ll-methyllanthionine and dl-lanthionine. The mature bibacillin 1 peptides showed cooperative bactericidal activity against Gram-positive bacteria, including members of the ESKAPE pathogens, and weak hemolytic activity. Optimal ratio studies suggest that bibacillin 1 works best when the components are present in a 1 : 1 r</pubmed_abstract><journal>RSC chemical biology</journal><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11385697</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Bibacillin 1: a two-component lantibiotic from &lt;i>Bacillus thuringiensis&lt;/i>.</pubmed_title><pmcid>PMC11385697</pmcid><funding_grant_id>S10 RR027109 A</funding_grant_id><funding_grant_id>R37GM058822</funding_grant_id><funding_grant_id>S10 RR027109</funding_grant_id><funding_grant_id>R37 GM058822</funding_grant_id><funding_grant_id>AI083214</funding_grant_id><funding_grant_id>P01 AI083214</funding_grant_id><pubmed_authors>Moreira R</pubmed_authors><pubmed_authors>Yang Y</pubmed_authors><pubmed_authors>Gilmore MS</pubmed_authors><pubmed_authors>Luo Y</pubmed_authors><pubmed_authors>van der Donk WA</pubmed_authors></additional><is_claimable>false</is_claimable><name>Bibacillin 1: a two-component lantibiotic from &lt;i>Bacillus thuringiensis&lt;/i>.</name><description>Here we describe bibacillin 1 - a two-component lantibiotic from &lt;i>Bacillus thuringiensis&lt;/i>. The peptides that comprise bibacillin 1 are modified by a class II lanthipeptide synthetase Bib1M producing two peptides with non-overlapping ring patterns that are reminiscent of cerecidin and the short component of the enterococcal cytolysin (CylL&lt;sub>S&lt;/sub>''), a virulence factor associated with human disease. Stereochemical analysis demonstrated that each component contains ll-methyllanthionine and dl-lanthionine. The mature bibacillin 1 peptides showed cooperative bactericidal activity against Gram-positive bacteria, including members of the ESKAPE pathogens, and weak hemolytic activity. Optimal ratio studies suggest that bibacillin 1 works best when the components are present in a 1 : 1 r</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Sep</publication><modification>2026-06-04T09:42:11.085Z</modification><creation>2025-04-21T14:55:29.141Z</creation></dates><accession>S-EPMC11385697</accession><cross_references><pubmed>39268544</pubmed><doi>10.1039/d4cb00192c</doi></cross_references></HashMap>