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Our previous work found that the depletion of lipopolysaccharide (LPS) export to the OM induces an essential PG remodeling process involving LD\u2010transpeptidases (LDTs), the glycosyltransferase function of PBP1B and the carboxypeptidase PBP6a. Consequently, cells with defective OM biogenesis lyse if they lack any of these PG enzymes. Here we report that the morphological defects, and lysis associated with a <jats:italic>ldtF<\/jats:italic> mutant with impaired LPS transport, are alleviated by the loss of the predicted OM\u2010anchored lipoprotein ActS (formerly YgeR). We show that ActS is an inactive member of LytM\u2010type peptidoglycan endopeptidases due to a degenerated catalytic domain. ActS is capable of activating all three main periplasmic peptidoglycan amidases, AmiA, AmiB, and AmiC, which were previously reported to be activated only by EnvC and\/or NlpD. Our data also suggest that in vivo ActS preferentially activates AmiC and that its function is linked to cell envelope stress.<\/jats:p>","DOI":"10.1111\/mmi.14712","type":"journal-article","created":{"date-parts":[[2021,3,4]],"date-time":"2021-03-04T13:00:31Z","timestamp":1614862831000},"page":"329-342","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":41,"title":["ActS activates peptidoglycan amidases during outer membrane stress in <i>Escherichia coli<\/i>"],"prefix":"10.1111","volume":"116","author":[{"given":"Carlos K.","family":"Gurnani Serrano","sequence":"first","affiliation":[{"name":"Dipartimento di Scienze Farmacologiche e Biomolecolari Universit\u00e0 degli Studi di Milano Milan Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthias","family":"Winkle","sequence":"additional","affiliation":[{"name":"The Centre for Bacterial Cell Biology Biosciences Institute Newcastle University Newcastle upon 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