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Beside the ability of RocS to bind DNA and interact with the chromosome partitioning protein ParB, little is known about how C\u2010terminal membrane anchor of RocS contributes to chromosome segregation. More precisely, the molecular basis of membrane targeting remains unresolved. This study addresses the interplay between RocS C\u2010terminal region and the lipid membrane. Combined magic\u2010angle spinning NMR and wide\u2010line NMR reveal that the membrane anchoring peptide folds into a short membrane\u2010inserted kink\u2010helix motif connected to an extended linker, with membrane insertion locally perturbing lipid packing. The fluidity of the lipid bilayer, modulated by temperature, in turn influences the anchor\u2010membrane interactions. At the mesoscale, AFM imaging shows that the anchor selectively associates with lipid nanodomains, clustering into discrete foci. Mutational studies further reveals that a single glycine mutation in the C\u2010terminal significantly perturbs chromosome segregation and alters lipid membrane properties. These findings reveal a mechanism for nanodomain association of a highly conserved membrane\u2010targeting motif in\n                    <jats:italic>Streptococci<\/jats:italic>\n                    , highlighting the kink\u2010helix anchor as a conserved element for membrane targeting across bacteria and beyond.\n                  <\/jats:p>","DOI":"10.1002\/advs.202521132","type":"journal-article","created":{"date-parts":[[2026,1,16]],"date-time":"2026-01-16T04:41:04Z","timestamp":1768538464000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Structural Basis of the Membrane Association by the Conserved RocS Membrane\u2010Targeting Sequence in\n                    <i>Streptococcus<\/i>"],"prefix":"10.1002","volume":"13","author":[{"given":"Ana","family":"\u00c1lvarez\u2010Mena","sequence":"first","affiliation":[{"name":"Univ. 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