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It is a gram\u2010negative bacterium with three groups of outer membrane proteins (OMPs): minor OMPs (Group 1) and major OMPs (Groups 2 and 3). OMPs with \u03b2\u2010barrel architecture play important roles in nutrient transport, efflux, adhesion, and membrane biogenesis. Despite their importance, the structure, function, and interaction dynamics of several\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>B. melitensis<\/jats:italic>\n                    <\/jats:styled-content>\n                    \u03b2\u2010barrel OMPs and associated protein complexes remain mostly unexplored. In this study, we conducted a comprehensive in silico analysis to characterize known outer membrane \u03b2\u2010barrel (OMBB) proteins and identify novel OMBBs in\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>B. melitensis<\/jats:italic>\n                    <\/jats:styled-content>\n                    16\u2009M. Proteins were modeled using five computational tools: AlphaFold 3, ESMFold, SWISS\u2010MODEL, RoseTTAFold, and TrRosetta. Outer\u2010membrane insertion of 12 novel OMBBs was confirmed using PPM 3.0, Protein GRAVY, DREAMM, and MemProtMD_Insane. Putative functions were predicted using structure\u2010 and sequence\u2010based annotations. Sequence variation across 46\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>B. melitensis<\/jats:italic>\n                    <\/jats:styled-content>\n                    strains was identified and mapped onto the structural models. OMBB\u2010associated protein complexes\u2014the RND (Resistance\u2010Nodulation\u2010Division) efflux pumps, the lipopolysaccharide transport (Lpt) complex, and the \u03b2\u2010barrel assembly machinery (BAM) complex\u2014were modeled, and protein\u2013protein interactions (PPIs) were analyzed to confirm thermodynamically stable assemblies. This study presents a robust in silico strategy for exploring OMP architecture and provides valuable structural insights to support the development of diagnostics, targeted therapeutics, and vaccines against\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>B. melitensis<\/jats:italic>\n                    <\/jats:styled-content>\n                    .\n                  <\/jats:p>","DOI":"10.1002\/prot.70118","type":"journal-article","created":{"date-parts":[[2026,1,26]],"date-time":"2026-01-26T08:50:36Z","timestamp":1769417436000},"page":"1279-1305","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Identification and Characterization of Outer Membrane Proteins and Membrane Spanning Protein Complexes in\n                    <scp>\n                      <i>Brucella melitensis<\/i>\n                    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