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Phosphorus exists in the environment in both organic and inorganic forms, with phosphate being the predominant form of inorganic phosphorus. SAR11 bacteria, a group of oligotrophic marine bacteria, possess high-affinity transporters for limiting nutrients such as phosphate, nitrogen, and organic carbon, enabling them to dominate in nutrient-depleted environments. Despite their ecological significance, the molecular mechanisms underlying phosphate transport and metabolism in SAR11 bacteria remain elusive. Here, we investigated the phosphate transport system in\n                      <jats:italic toggle=\"yes\">Candidatus<\/jats:italic>\n                      Pelagibacter sp. HTCC7211, a representative SAR11 bacterium, which encodes an ATP-binding cassette-type phosphate transporter,\n                      <jats:italic toggle=\"yes\">Cp<\/jats:italic>\n                      PstSCAB. We heterologously expressed and purified\n                      <jats:italic toggle=\"yes\">Cp<\/jats:italic>\n                      PstS, the substrate-binding component of the transporter, and determined its crystal structure in complex with phosphate to gain insights into its substrate recognition mechanism. Microscale thermophoresis binding assays demonstrated that\n                      <jats:italic toggle=\"yes\">Cp<\/jats:italic>\n                      PstS binds phosphate with high affinity, exhibiting a dissociation constant (\n                      <jats:italic toggle=\"yes\">K<\/jats:italic>\n                      <jats:sub>\n                        <jats:italic toggle=\"yes\">d<\/jats:italic>\n                      <\/jats:sub>\n                      ) of 112 nM. Phylogenetic analysis placed\n                      <jats:italic toggle=\"yes\">Cp<\/jats:italic>\n                      PstS in a distinct branch of previously characterized PstS proteins. Structural analysis further revealed that\n                      <jats:italic toggle=\"yes\">Cp<\/jats:italic>\n                      PstS employs a unique binding site and a distinct hydrogen-bonding network for phosphate recognition and features an expanded substrate-binding cavity, suggesting potential for organic phosphorus binding. The bioinformatic analysis further indicated that\n                      <jats:italic toggle=\"yes\">Cp<\/jats:italic>\n                      PstS-type phosphate-binding proteins are widely distributed among SAR11 bacteria. These findings provide valuable insights into phosphorus acquisition and utilization mechanisms in SAR11 bacteria, enhancing our understanding of their adaptation to nutrient-limited marine environments.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        This study provides crucial insights into phosphate acquisition in SAR11 bacteria, a key group of oligotrophic microorganisms that thrive in nutrient-limited marine ecosystems. By characterizing the unique structural features of\n                        <jats:italic toggle=\"yes\">Cp<\/jats:italic>\n                        PstS, including its distinct hydrogen-bonding network and expanded substrate-binding cavity, this research sheds light on how SAR11 bacteria adapt to limited phosphorus availability. The discovery that\n                        <jats:italic toggle=\"yes\">Cp<\/jats:italic>\n                        PstS may also accommodate organic phosphorus compounds broadens our understanding of microbial nutrient acquisition. These findings have significant implications for marine biogeochemical cycles and offer new perspectives on the evolution of nutrient transport mechanisms in marine microorganisms.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/mbio.01654-25","type":"journal-article","created":{"date-parts":[[2025,8,13]],"date-time":"2025-08-13T13:01:01Z","timestamp":1755090061000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":3,"title":["Structural and molecular basis for phosphate recognition by SAR11 bacteria"],"prefix":"10.1128","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0009-0000-6133-9014","authenticated-orcid":false,"given":"Wen-Jing","family":"Zhu","sequence":"first","affiliation":[{"name":"MOE Key Laboratory of Evolution and Marine Biodiversity, Frontiers Science Center for Deep Ocean Multispheres and Earth System and College of Marine Life Sciences, Ocean University of China","place":["Qingdao, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chen","family":"Wang","sequence":"additional","affiliation":[{"name":"MOE Key Laboratory of Evolution and Marine Biodiversity, Frontiers Science Center for Deep Ocean Multispheres and Earth System and College of Marine Life Sciences, Ocean University of China","place":["Qingdao, China"]},{"name":"Marine Biotechnology Research Center, State Key Laboratory of Microbial Technology, Shandong University","place":["Qingdao, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li","family":"Liu","sequence":"additional","affiliation":[{"name":"Marine Biotechnology Research Center, State Key Laboratory of Microbial Technology, Shandong University","place":["Qingdao, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jian-Xun","family":"Li","sequence":"additional","affiliation":[{"name":"Marine Biotechnology Research Center, State Key Laboratory of Microbial Technology, Shandong University","place":["Qingdao, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hou-Qi","family":"Wang","sequence":"additional","affiliation":[{"name":"MOE Key Laboratory of Evolution and Marine Biodiversity, Frontiers Science Center for Deep Ocean Multispheres and Earth System and College of Marine Life Sciences, Ocean University of China","place":["Qingdao, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meng-Qi","family":"Wang","sequence":"additional","affiliation":[{"name":"MOE Key Laboratory of Evolution and Marine Biodiversity, Frontiers Science Center for Deep Ocean Multispheres and Earth System and College of Marine Life Sciences, Ocean University of China","place":["Qingdao, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hai-Yan","family":"Cao","sequence":"additional","affiliation":[{"name":"MOE Key Laboratory of Evolution and Marine Biodiversity, Frontiers 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