{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Anlauf MT"],"funding":["Deutsche Forschungsgemeinschaft","Heinrich-Heine-Universität Düsseldorf"],"pagination":["8994"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11026475"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(1)"],"pubmed_abstract":["Type I secretion systems (T1SS) facilitate the secretion of substrates in one step across both membranes of Gram-negative bacteria. A prime example is the hemolysin T1SS which secretes the toxin HlyA. Secretion is energized by the ABC transporter HlyB, which forms a complex together with the membrane fusion protein HlyD and the outer membrane protein TolC. HlyB features three domains: an N-terminal C39 peptidase-like domain (CLD), a transmembrane domain (TMD) and a C-terminal nucleotide binding domain (NBD). Here, we created chimeric transporters by swapping one or more domains of HlyB with the respective domain(s) of RtxB, a HlyB homolog from Kingella kingae. We tested all chimeric transporters for their ability to secrete pro-HlyA when co-expressed with HlyD. The CLD proved to be most cr"],"journal":["Scientific reports"],"pubmed_title":["Type 1 secretion necessitates a tight interplay between all domains of the ABC transporter."],"pmcid":["PMC11026475"],"funding_grant_id":["INST 208/761-1 FUGG","CRC 1208 project A01","Grant number 417919780"],"pubmed_authors":["Reiners J","Spitz O","Bilsing FL","Smits SHJ","Schmitt L","Anlauf MT","Hachani E"],"additional_accession":[]},"is_claimable":false,"name":"Type 1 secretion necessitates a tight interplay between all domains of the ABC transporter.","description":"Type I secretion systems (T1SS) facilitate the secretion of substrates in one step across both membranes of Gram-negative bacteria. A prime example is the hemolysin T1SS which secretes the toxin HlyA. Secretion is energized by the ABC transporter HlyB, which forms a complex together with the membrane fusion protein HlyD and the outer membrane protein TolC. HlyB features three domains: an N-terminal C39 peptidase-like domain (CLD), a transmembrane domain (TMD) and a C-terminal nucleotide binding domain (NBD). Here, we created chimeric transporters by swapping one or more domains of HlyB with the respective domain(s) of RtxB, a HlyB homolog from Kingella kingae. We tested all chimeric transporters for their ability to secrete pro-HlyA when co-expressed with HlyD. The CLD proved to be most cr","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-06-01T09:18:59.485Z","creation":"2026-04-08T11:02:33.6Z"},"accession":"S-EPMC11026475","cross_references":{"pubmed":["38637678"],"doi":["10.1038/s41598-024-59759-0"]}}