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The most abundant encapsulin cargo class are Dye\u2010decolorizing Peroxidases (DyPs). It has been previously suggested that DyP encapsulins are involved in oxidative stress resistance and bacterial pathogenicity due to DyPs\u2019 inherent ability to reduce and detoxify hydrogen peroxide while oxidizing a broad range of organic co\u2010substrates. Here, we report the structural and biochemical analysis of a DyP encapsulin widely found across enterobacteria. Using bioinformatic approaches, we show that this DyP encapsulin is encoded by a conserved transposon\u2010associated operon, enriched in enterobacterial pathogens. Through low pH and peroxide exposure experiments, we highlight the stability of this DyP encapsulin under harsh conditions and show that DyP catalytic activity is highest at low pH. We determine the structure of the DyP\u2010loaded shell and free DyP via cryo\u2010electron microscopy, revealing the structural basis for DyP cargo loading and peroxide preference. This work lays the foundation to further explore the substrate range and physiological functions of enterobacterial DyP encapsulins.<\/jats:p>","DOI":"10.1002\/advs.202415827","type":"journal-article","created":{"date-parts":[[2025,4,2]],"date-time":"2025-04-02T09:29:14Z","timestamp":1743586154000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Structural and Biochemical Characterization of a Widespread Enterobacterial Peroxidase Encapsulin"],"prefix":"10.1002","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0411-8674","authenticated-orcid":false,"given":"Natalia C.","family":"Ubilla\u2010Rodriguez","sequence":"first","affiliation":[{"name":"Department of Biological Chemistry University of Michigan Medical School  Ann Arbor MI 48109 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8871-3053","authenticated-orcid":false,"given":"Michael 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