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Previous studies have shown that calcium (Ca\n                      <jats:sup>2+<\/jats:sup>\n                      ) at the levels encountered during infections increases\n                      <jats:italic toggle=\"yes\">Pa<\/jats:italic>\n                      resistance to PMB. However, the mechanisms of this Ca\n                      <jats:sup>2+<\/jats:sup>\n                      regulation are not known. Here, we identified three novel genes (\n                      <jats:italic toggle=\"yes\">PA2803, PA3237<\/jats:italic>\n                      , and\n                      <jats:italic toggle=\"yes\">PA5317<\/jats:italic>\n                      ) that contribute to the Ca\n                      <jats:sup>2+<\/jats:sup>\n                      -dependent PMB resistance in\n                      <jats:italic toggle=\"yes\">Pa. PA2803<\/jats:italic>\n                      , the focus of this work, encodes a putative phosphonatase and is a founding member of the PA2803 subfamily from the Haloacid Dehalogenase Superfamily. Since the transcription of this gene is regulated by both Ca\n                      <jats:sup>2+<\/jats:sup>\n                      and inorganic phosphate (P\n                      <jats:sub>i<\/jats:sub>\n                      ), we named it \u201cP\n                      <jats:sub>i<\/jats:sub>\n                      and Ca\n                      <jats:sup>2+<\/jats:sup>\n                      -regulated protein, PcrP.\u201d Congruent with sequence-based predictions, we showed that PcrP lacks catalytic activity and instead binds protein partners, revealing a novel non-catalytic function. By using pull-down assays and bacterial two-hybrid systems, we identified and validated two protein partners of PcrP: Acp3 and PA3518. We showed that PcrP is involved in oxidative stress responses in\n                      <jats:italic toggle=\"yes\">Pa<\/jats:italic>\n                      , which are likely mediated by its interactions with Acp3 and may support its role in PMB resistance. In addition, PcrP imparts a Ca\n                      <jats:sup>2+<\/jats:sup>\n                      -dependent growth advantage during P\n                      <jats:sub>i<\/jats:sub>\n                      starvation and plays a role in polyphosphate accumulation in a Ca\n                      <jats:sup>2+<\/jats:sup>\n                      -dependent manner. Overall, this study identified a novel protein-binding function for the PA2803 subfamily representative, which mediates\n                      <jats:italic toggle=\"yes\">Pa<\/jats:italic>\n                      responses to elevated Ca\n                      <jats:sup>2+<\/jats:sup>\n                      and P\n                      <jats:sub>i<\/jats:sub>\n                      starvation and enhances PMB resistance.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        <jats:italic toggle=\"yes\">Pseudomonas aeruginosa<\/jats:italic>\n                        (\n                        <jats:italic toggle=\"yes\">Pa<\/jats:italic>\n                        ) is a critical human pathogen that presents significant clinical challenges, underscoring the urgent need for understanding its resistance mechanisms. Previous studies have shown that calcium (Ca\n                        <jats:sup>2+<\/jats:sup>\n                        ) at the levels detected during infections increases\n                        <jats:italic toggle=\"yes\">Pa<\/jats:italic>\n                        resistance to the last resort antibiotic polymyxin B (PMB). For the first time, we identified three novel genes, whose products are required for the Ca\n                        <jats:sup>2+<\/jats:sup>\n                        -dependent PMB resistance in\n                        <jats:italic toggle=\"yes\">Pa<\/jats:italic>\n                        . One of them,\n                        <jats:italic toggle=\"yes\">PA2803<\/jats:italic>\n                        , regulated by Ca\n                        <jats:sup>2+<\/jats:sup>\n                        and phosphate, was named phosphate and Ca\n                        <jats:sup>2+<\/jats:sup>\n                        -regulated protein, PcrP. This study discovered a novel protein-binding function of PcrP and identified two protein partners. Given the high level of sequence conservation within the PA2803 subfamily, the protein-binding function may be shared by other members of the PA2803 subfamily.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/jb.00189-25","type":"journal-article","created":{"date-parts":[[2025,10,17]],"date-time":"2025-10-17T13:12:58Z","timestamp":1760706778000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":2,"title":["The PA2803-encoded PcrP exhibits a novel non-catalytic function and contributes to polymyxin B resistance in\n                    <i>P. aeruginosa<\/i>"],"prefix":"10.1128","volume":"207","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3711-5501","authenticated-orcid":true,"given":"T.","family":"Salpadoru","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01g9vbr38","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Microbiology and Molecular Genetics, Oklahoma State University","place":["Stillwater, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S.","family":"Khanam","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01g9vbr38","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Microbiology and Molecular Genetics, Oklahoma State University","place":["Stillwater, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V. 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