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By modulating a single growth parameter\u2014extracellular pH\u2014we discovered a subset of these so-called \u2018redundant\u2019 enzymes in Escherichia coli are required for maximal fitness across pH environments. Among these pH specialists are the class A penicillin binding proteins PBP1a and PBP1b; defects in these enzymes attenuate growth in alkaline and acidic conditions, respectively. Genetic, biochemical, and cytological studies demonstrate that synthase activity is required for cell wall integrity across a wide pH range and influences pH-dependent changes in resistance to cell wall active antibiotics. Altogether, our findings reveal previously thought to be redundant enzymes are instead specialized for distinct environmental niches. This specialization may ensure robust growth and cell wall integrity in a wide range of conditions.<\/jats:p>\n                  <jats:p>Editorial note: This article has been through an editorial process in which the authors decide how to respond to the issues raised during peer review. The Reviewing Editor's assessment is that all the issues have been addressed (see decision letter).<\/jats:p>","DOI":"10.7554\/elife.40754","type":"journal-article","created":{"date-parts":[[2019,4,8]],"date-time":"2019-04-08T20:00:35Z","timestamp":1554753635000},"source":"Crossref","is-referenced-by-count":99,"title":["Plasticity of Escherichia coli cell wall metabolism promotes fitness and antibiotic resistance across environmental conditions"],"prefix":"10.7554","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5482-6551","authenticated-orcid":true,"given":"Elizabeth A","family":"Mueller","sequence":"first","affiliation":[{"name":"Department of Biology, Washington University in St. Louis, St. Louis, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander JF","family":"Egan","sequence":"additional","affiliation":[{"name":"Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon 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