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Pathogenic\n                      <jats:italic toggle=\"yes\">Chlamydia<\/jats:italic>\n                      species are unusual in lacking a peptidoglycan sacculus, yet they do synthesize a transient and localized peptidoglycan structure at the divisome of the RB during their polarized division process. Although several studies have described the components of the chlamydial divisome necessary to generate peptidoglycan at a specific site on the membrane, less is understood about how the peptidoglycan structure is degraded to allow for the daughter cell to form and the division process to complete. Amidases are key components of the cell wall in model system bacteria as they catalyze the degradation and remodeling of peptidoglycan, including in the division septum. Here, we characterized the cell division-associated amidase, AmiA_Ct, of\n                      <jats:italic toggle=\"yes\">Chlamydia trachomatis<\/jats:italic>\n                      both\n                      <jats:italic toggle=\"yes\">in vitro<\/jats:italic>\n                      and\n                      <jats:italic toggle=\"yes\">in vivo<\/jats:italic>\n                      . Our\n                      <jats:italic toggle=\"yes\">in vitro<\/jats:italic>\n                      data show that AmiA_Ct is a\n                      <jats:italic toggle=\"yes\">bona fide<\/jats:italic>\n                      , metal-dependent amidase capable of cleaving peptidoglycan. AmiA_Ct complemented an\n                      <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                      amidase-deficient strain and supported the growth and separation of daughter cells. To assess the function of AmiA_Ct in\n                      <jats:italic toggle=\"yes\">C. trachomatis<\/jats:italic>\n                      , we generated a transformant strain carrying an inducible CRISPR interference system targeting the\n                      <jats:italic toggle=\"yes\">amiA<\/jats:italic>\n                      gene. Knocking down expression of\n                      <jats:italic toggle=\"yes\">amiA<\/jats:italic>\n                      resulted in altered bacterial morphology, a reduction in infectious EBs, and the accumulation of peptidoglycan in the organisms. These data indicate a critical function for AmiA_Ct in the unique cell division process of\n                      <jats:italic toggle=\"yes\">Chlamydia<\/jats:italic>\n                      .\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>IMPORTANCE<\/jats:title>\n                    <jats:p>\n                      Peptidoglycan is an important structural cell wall polymer that serves to give bacteria their shape and resistance to changes in extracellular solute concentrations. For\n                      <jats:italic toggle=\"yes\">Chlamydia trachomatis<\/jats:italic>\n                      , an obligate intracellular pathogen that divides within a host cell, peptidoglycan is only used for cell division and is not a component of its cell wall. In this study, we characterize the function of a chlamydial amidase that helps degrade peptidoglycan during cell division. We show a critical function for amidase activity in facilitating changes to the peptidoglycan structure during chlamydial cell division that support normal growth and development of this pathogenic bacterium.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/jb.00453-25","type":"journal-article","created":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T13:42:21Z","timestamp":1773236541000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["Characterization of the cell division-associated peptidoglycan amidase AmiA of\n                    <i>Chlamydia trachomatis<\/i>"],"prefix":"10.1128","volume":"208","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2688-2796","authenticated-orcid":false,"given":"Julia","family":"Dannenberg","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01xnwqx93","id-type":"ROR","asserted-by":"publisher"}],"name":"Institute for 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