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Amidases play a vital role in septal cell wall cleavage and help separate daughter cells during cell division. Most amidases are zinc metalloenzymes, and <jats:italic>E. coli<\/jats:italic> cells lacking amidases grow as chains with daughter cells attached to each other. In this study, we have characterized two amidase enzymes from <jats:italic>Deinococcus indicus<\/jats:italic> DR1. <jats:italic>D. indicus<\/jats:italic> DR1 is known for its high arsenic tolerance and unique cell envelope. However, details of their cell wall biogenesis remain largely unexplored.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Results<\/jats:title>\n                <jats:p>We have characterized two amidases Ami1<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> and Ami2<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> from <jats:italic>D. indicus<\/jats:italic> DR1. Both Ami1<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> and Ami2<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> suppress cell separation defects in <jats:italic>E. coli<\/jats:italic> amidase mutants, suggesting that these enzymes are able to cleave septal cell wall. Ami1<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> and Ami2<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> proteins possess the Amidase_3 catalytic domain with conserved \u2013GHGG- motif and Zn<jats:sup>2+<\/jats:sup> binding sites. Zn<jats:sup>2+<\/jats:sup>- binding in Ami1<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> is crucial for amidase activity. AlphaFold2 structures of both Ami1<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> and Ami2<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> were predicted, and Ami1<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> was a closer homolog to AmiA of <jats:italic>E. coli<\/jats:italic>.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Conclusion<\/jats:title>\n                <jats:p>Our results indicate that Ami1<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> and Ami2<jats:sub><jats:italic>Di<\/jats:italic><\/jats:sub> enzymes can cleave peptidoglycan, and structural prediction studies revealed insights into the activity and regulation of these enzymes in <jats:italic>D. indicus<\/jats:italic> DR1.<\/jats:p>\n              <\/jats:sec>","DOI":"10.1186\/s12866-024-03225-4","type":"journal-article","created":{"date-parts":[[2024,3,26]],"date-time":"2024-03-26T10:02:10Z","timestamp":1711447330000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Structure predictions and functional insights into Amidase_3 domain containing N-acetylmuramyl-L-alanine amidases from Deinococcus indicus DR1"],"prefix":"10.1186","volume":"24","author":[{"given":"Malvika","family":"Modi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Menaka","family":"Thambiraja","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Archana","family":"Cherukat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ragothaman M","family":"Yennamalli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richa","family":"Priyadarshini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,3,26]]},"reference":[{"key":"3225_CR1","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1111\/j.1574-6976.2007.00094.x","volume":"32","author":"W Vollmer","year":"2008","unstructured":"Vollmer W, Blanot D, De Pedro MA. 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