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SanA, an inner membrane protein in\n                      <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                      K-12, is required for vancomycin resistance at high temperatures (&gt;42\u00b0C) and impacts sodium dodecyl sulfate (SDS) resistance during the stationary phase reached from carbon limitation. However, its function remains unknown. Here, we show that \u0394\n                      <jats:italic toggle=\"yes\">sanA<\/jats:italic>\n                      has a synthetic genetic interaction with \u0394\n                      <jats:italic toggle=\"yes\">wecA<\/jats:italic>\n                      , a mutation that increases the availability of the isoprenoid carrier for PG synthesis. Specifically, the \u0394\n                      <jats:italic toggle=\"yes\">sanA<\/jats:italic>\n                      \u0394\n                      <jats:italic toggle=\"yes\">wecA<\/jats:italic>\n                      strain demonstrated heightened SDS-EDTA sensitivity, activation of the Rcs stress response, and increased cell length. Further investigation tied the SDS-EDTA sensitivity to increased lipid II available for PG synthesis. Spontaneous suppressor mutants of this phenotype harbored point mutations in\n                      <jats:italic toggle=\"yes\">prc<\/jats:italic>\n                      , which encodes tail-specific protease, or\n                      <jats:italic toggle=\"yes\">ftsI<\/jats:italic>\n                      , which encodes the cell division DD-transpeptidase, a target of Prc. We focused on the\n                      <jats:italic toggle=\"yes\">ftsI<\/jats:italic>\n                      mutations and demonstrated that the\n                      <jats:italic toggle=\"yes\">ftsI<\/jats:italic>\n                      mutations increased cell length but nevertheless enhanced PG incorporation at the septum compared to the \u0394\n                      <jats:italic toggle=\"yes\">sanA<\/jats:italic>\n                      mutant, returning PG incorporation to wild-type levels. Moreover, other mutations affecting septal PG synthesis, but not divisome assembly, also suppressed the SDS-EDTA sensitivity. These findings suggest that in the absence of SanA, increased lipid II availability perturbs the balance between septal PG synthesis, lateral PG elongation, and other envelope biogenesis pathways, leading to increased OM permeability.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        The gram-negative cell envelope is a barrier that protects the cell from environmental stress. Therefore, the synthesis of each layer of this envelope needs to be closely coordinated throughout growth and division. Here, we investigated SanA, a protein in\n                        <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                        K-12 that affects envelope permeability under cellular stress, including nutrient limitation and high temperature. We found that SanA plays a key role in maintaining the permeability barrier when precursor levels for peptidoglycan (PG) synthesis are elevated, linking envelope integrity to balanced septal PG production during cell division. Our results suggest that SanA modulates substrate availability to preserve envelope function, and that in its absence, imbalanced substrate flux to septal PG synthesis disrupts septum formation and compromises barrier integrity.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/mbio.00635-26","type":"journal-article","created":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T13:02:48Z","timestamp":1777554168000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["Impaired envelope integrity in the absence of SanA is linked to increased lipid II availability and an imbalance of septal peptidoglycan synthesis"],"prefix":"10.1128","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9228-8168","authenticated-orcid":false,"given":"Joseph F.","family":"Carr","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01f5ytq51","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Texas A&M University","place":["College Station, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carolina","family":"Basurto De Santiago","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01f5ytq51","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Texas A&M University","place":["College Station, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shivani A.","family":"Bhut","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01f5ytq51","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Texas A&M University","place":["College Station, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel J.","family":"Warzecha","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01f5ytq51","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Texas A&M University","place":["College Station, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah A.","family":"Vastani","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01f5ytq51","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Texas A&M University","place":["College Station, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert","family":"Wei","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01f5ytq51","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Texas A&M University","place":["College Station, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carmen M.","family":"Herrera","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases, College of Veterinary Medicine, University of Georgia","place":["Athens, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6134-1800","authenticated-orcid":true,"given":"M. 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