A novel peptidoglycan deacetylase modulates daughter cell separation in E. coli.

ABSTRACT: Peptidoglycan hydrolases facilitate bacterial cell wall growth by creating space for insertion of new material and allowing physical separation of daughter cells. In Escherichia coli, three peptidoglycan amidases, AmiA, AmiB and AmiC, cleave septal peptidoglycan during cell division. The LytM-domain proteins EnvC, NlpD and ActS activate these amidases either from inside the cell or the outer membrane: EnvC binds to the cytoplasmic membrane-anchored divisome components FtsEX, while NlpD and ActS are outer membrane-anchored lipoproteins. Here we report the identification of a novel periplasmic deacetylase called SddA that removes acetyl groups from denuded peptidoglycan glycan strands, the products of amidases. The sddA gene is co-expressed with the gene encoding EnvC, linking SddA function

SUBMITTER: Hernandez-Rocamora VM 

PROVIDER: S-EPMC12440217 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature