{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Selim KA"],"funding":["Bundesministerium für Bildung und Forschung","Deutsche Forschungsgemeinschaft"],"pagination":["e2205882120"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9974498"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["120(8)"],"pubmed_abstract":["The PII superfamily consists of widespread signal transduction proteins found in all domains of life. In addition to canonical PII proteins involved in C/N sensing, structurally similar PII-like proteins evolved to fulfill diverse, yet poorly understood cellular functions. In cyanobacteria, the bicarbonate transporter SbtA is co-transcribed with the conserved PII-like protein, SbtB, to augment intracellular inorganic carbon levels for efficient CO<sub>2</sub> fixation. We identified SbtB as a sensor of various adenine nucleotides including the second messenger nucleotides cyclic AMP (cAMP) and c-di-AMP. Moreover, many SbtB proteins possess a C-terminal extension with a disulfide bridge of potential redox-regulatory function, which we call R-loop. Here, we reveal an unusual ATP/ADP apyrase "],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Carbon signaling protein SbtB possesses atypical redox-regulated apyrase activity to facilitate regulation of bicarbonate transporter SbtA."],"pmcid":["PMC9974498"],"funding_grant_id":["PRO-SELIM-2022-14","SPP1879"],"pubmed_authors":["Forchhammer K","Selim KA","Haffner M","Hagemann M","Zhu H","Albrecht R","Mantovani O","Hartmann MD"],"additional_accession":[]},"is_claimable":false,"name":"Carbon signaling protein SbtB possesses atypical redox-regulated apyrase activity to facilitate regulation of bicarbonate transporter SbtA.","description":"The PII superfamily consists of widespread signal transduction proteins found in all domains of life. In addition to canonical PII proteins involved in C/N sensing, structurally similar PII-like proteins evolved to fulfill diverse, yet poorly understood cellular functions. In cyanobacteria, the bicarbonate transporter SbtA is co-transcribed with the conserved PII-like protein, SbtB, to augment intracellular inorganic carbon levels for efficient CO<sub>2</sub> fixation. We identified SbtB as a sensor of various adenine nucleotides including the second messenger nucleotides cyclic AMP (cAMP) and c-di-AMP. Moreover, many SbtB proteins possess a C-terminal extension with a disulfide bridge of potential redox-regulatory function, which we call R-loop. Here, we reveal an unusual ATP/ADP apyrase ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2026-05-29T07:45:20.938Z","creation":"2025-02-19T01:18:04.998Z"},"accession":"S-EPMC9974498","cross_references":{"pubmed":["36800386"],"doi":["10.1073/pnas.2205882120"]}}