{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dai Y"],"funding":["Umea University","The laboratory of Molecular Infection Medicine Sweden","NIAID NIH HHS","Knut och Alice Wallenbergs Stiftelse","HHS | NIH | National Institute of Allergy and Infectious Diseases","Kempestiftelserna","Swedish Research Council","Northeastern University"],"pagination":["e0278621"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8649774"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(6)"],"pubmed_abstract":["The hospital-acquired pathogen Acinetobacter baumannii possesses a complex cell envelope that is key to its multidrug resistance and virulence. The bacterium, however, lacks many canonical enzymes that build the envelope in model organisms. Instead, A. baumannii contains a number of poorly annotated proteins that may allow alternative mechanisms of envelope biogenesis. We demonstrated previously that one of these unusual proteins, ElsL, is required for maintaining a characteristic short rod shape and for withstanding antibiotics that attack the septal cell wall. Curiously, ElsL is composed of a leaderless YkuD-family domain usually found in secreted, cell wall-modifying l,d-transpeptidases (LDTs). Here, we show that, rather than being an LDT, ElsL is actually a new class of cytoplasmic l,d"],"journal":["mBio"],"pubmed_title":["A New Class of Cell Wall-Recycling l,d-Carboxypeptidase Determines β-Lactam Susceptibility and Morphogenesis in Acinetobacter baumannii."],"pmcid":["PMC8649774"],"funding_grant_id":["R01AI162996","R01 AI162996"],"pubmed_authors":["Geisinger E","Tang AY","Cava F","Dai Y","Pinedo V"],"additional_accession":[]},"is_claimable":false,"name":"A New Class of Cell Wall-Recycling l,d-Carboxypeptidase Determines β-Lactam Susceptibility and Morphogenesis in Acinetobacter baumannii.","description":"The hospital-acquired pathogen Acinetobacter baumannii possesses a complex cell envelope that is key to its multidrug resistance and virulence. The bacterium, however, lacks many canonical enzymes that build the envelope in model organisms. Instead, A. baumannii contains a number of poorly annotated proteins that may allow alternative mechanisms of envelope biogenesis. We demonstrated previously that one of these unusual proteins, ElsL, is required for maintaining a characteristic short rod shape and for withstanding antibiotics that attack the septal cell wall. Curiously, ElsL is composed of a leaderless YkuD-family domain usually found in secreted, cell wall-modifying l,d-transpeptidases (LDTs). Here, we show that, rather than being an LDT, ElsL is actually a new class of cytoplasmic l,d","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Dec","modification":"2026-06-12T10:27:52.432Z","creation":"2022-02-11T15:39:59.562Z"},"accession":"S-EPMC8649774","cross_references":{"pubmed":["34872350"],"doi":["10.1128/mBio.02786-21"]}}