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Universal stress proteins (USP) are key molecular components that enable bacterial adaptation and persistence under these challenging conditions. In this study, we investigated the diversity, structural features, and evolutionary dynamics of USP genes across 13 type strains of\n                    <jats:italic>Liquorilactobacillus<\/jats:italic>\n                    species. A total of 65\n                    <jats:italic>usp<\/jats:italic>\n                    -encoding genes were identified, ranging from three to six copies per genome, all predicted to be cytoplasmic and exhibiting the conserved Usp fold. Phylogenetic analysis revealed that Usp diversification resulted primarily from ancestral gene duplication events followed by gene losses, with no evidence of recent lineage-specific expansions. Approximately half of the proteins retained a canonical ATP-binding motif, while others lacked it or contained degenerate variants, suggesting an evolutionary trajectory from an ancestral non-ATP-binding form toward a gain-of-function motif. Codon-level selection analysis indicated strong purifying selection acting on most sites, with substitutions concentrated in loop regions that may contribute to functional divergence. A focused analysis of\n                    <jats:italic>Liquorilactobacillus vini<\/jats:italic>\n                    revealed structural and sequence heterogeneity among its five Usp paralogs, correlating with differential stress-response expression patterns. Overall, our findings demonstrate that Usp evolution in\n                    <jats:italic>Liquorilactobacillus<\/jats:italic>\n                    reflects a balance between conservation and diversification, highlighting their central role in stress adaptation and ecological success in dynamic fermentation environments.\n                  <\/jats:p>","DOI":"10.1007\/s11274-026-04821-4","type":"journal-article","created":{"date-parts":[[2026,2,28]],"date-time":"2026-02-28T06:10:44Z","timestamp":1772259044000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Diversity and evolutionary dynamics of universal stress proteins in the Liquorilactobacillus genus"],"prefix":"10.1007","volume":"42","author":[{"given":"Dayane da Silva","family":"Santos","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Allyson Andrade","family":"Mendon\u00e7a","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nara Suzy Aguiar","family":"Freitas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9727-0300","authenticated-orcid":false,"given":"Marcos Ant\u00f4nio","family":"De Morais Jr","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,2,28]]},"reference":[{"issue":"1","key":"4821_CR1","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1002\/prot.10064","volume":"48","author":"L Aravind","year":"2002","unstructured":"Aravind L, Anantharaman V, Koonin EV (2002) Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA world. 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