GPMDB00235OtherLiu T, et al.InstrumentNot AvailableNot availableSinorhizobium_fredii_hh103, Sinorhizobium_meliloti_1021, Sinorhizobium_meliloti_ak83cftian@cau.edu.cn26401955State Key Laboratory of Agrobiotechnology, and College of Biological Sciences, China Agricultural Universityhttp://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320018836Not availableGPMDBSinorhizobium meliloti, a facultative microsymbiont of alfalfa, should fine-tune its cellular processes to live saprophytically in soils characterized with limited nutrients and diverse stresses. In this study, TiO2 enrichment and LC-MS/MS were used to uncover the site-specific Ser/Thr/Tyr phosphoproteome of S. meliloti in minimum medium at stationary phase. There are a total of 96 unique phosphorylated sites, with a Ser/Thr/Tyr distribution of 63:28:5, in 77 proteins. Phosphoproteins identified in S. meliloti showed a wide distribution pattern regarding to functional categories, such as replication, transcription, translation, posttranslational modification, transport and metabolism of amino acids, carbohydrate, inorganic ion, succinoglycan etc. Ser/Thr/Tyr phosphosites identified within the conserved motif in proteins of key cellular function indicate a crucial role of phosphorylation in modulating cellular physiology. Moreover, phosphorylation in proteins involved in processes related to rhizobial adaptation was also discussed, such as those identified in SMa0114 and PhaP2 (polyhydroxybutyrate synthesis), ActR (pH stress and microaerobic adaption), SupA (potassium stress), chaperonin GroEL2 (viability and potentially symbiosis), and ExoP (succinoglycan synthesis and secretion). These Ser/Thr/Tyr phosphosites identified herein would be helpful for our further investigation and understanding of the role of phosphorylation in rhizobial physiology.Site-Specific Ser/Thr/Tyr Phosphoproteome of Sinorhizobium meliloti at Stationary Phase.Liu Tao T,Tian Chang Fu CF,Chen Wen Xin WX,Liu Tao T, Tian Chang Fu CF, Chen Wen Xin WXTyrosine, SER, Rhizobium meliloti, stationary phase, G1/G0 transition, Siglec-1, tirosina, establishment of cell quiescence., Tyr, Ensifer meliloti, 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, smooth ER, 2-Amino-3-(p-hydroxyphenyl)propionic acid, cell cycle quiescence, Sialic acid-binding Ig-like lectin 1, Tyrosin, C9H11NO3, Sheep erythrocyte receptor, CD169projections, liquid chromatography tandem mass spectroscopy, PLXN5, Slf, lamellae, Somatomedin-C, Nl1, nutrient medium, alfalfa, FPH2, PLEXIN-B1, Sialic acid-binding Ig-like lectin 1, process of organ, SeP, LC-MS-MS, protrusion, lamella, G1/G0 transition, CEH, Ensifer meliloti, LC-MSMS, smooth ER, NEPII, NL1, NL2, SEH, SEP, SER, study, LCMSMS, Siglec-1, nutrients, 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, somatomedin-C, SF, Kitl, ridges, Medicago sativa subsp. sativa, Mast cell growth factor, sEP, IGF1, papilla, Tyr, Mechano growth factor, SELP, lucerne, Soluble KIT ligand, Tyrosin, Sl, laminae, CD169, LC-MS2, IGF-I, data, steel factor, anatomical protrusion, hematopoietic growth factor KL, anatomical process, lamina, LC-MS/MS, 2-Amino-3-(p-hydroxyphenyl)propionic acid, cell cycle quiescence, somatomedin, flanges, Mell1, sKITLG, Tyrosine, LC/MS/MS, MMEL2, tirosina, mechano growth factor, shelf, Igf-1, flange, organ process, Rhizobium meliloti, SHEP7, mast cell growth factor, medium, growth medium, shelves, Stem cell factor, C9H11NO3, STAT5, projection, Sheep erythrocyte receptor, ridge, process, processes, stem cell factor, stationary phase, KL-1, spine, liquid chromatography-tandem mass spectroscopy, establishment of cell quiescence., MGF, c-Kit ligand, KITLG, processus, liquid chromatography tandem mass spectrometry, Eph2, SCF, NEP2Tyrosine, SER, Rhizobium meliloti, stationary phase, G1/G0 transition, Siglec-1, tirosina, establishment of cell quiescence., Tyr, Ensifer meliloti, 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, smooth ER, 2-Amino-3-(p-hydroxyphenyl)propionic acid, cell cycle quiescence, Sialic acid-binding Ig-like lectin 1, Tyrosin, C9H11NO3, Sheep erythrocyte receptor, CD169projections, liquid chromatography tandem mass spectroscopy, biochemical pathways, protein translation, Metabolic Process, posttranslational modification, InChI=1S/K, pCip, pCIP, supply, Aminosaeure, Metabolic Concepts, nutrient medium, hydrates de carbone, Sialic acid-binding Ig-like lectin 1, potasio, glucide, phosphorylation, carbohydrates, solute:solute exchange, Readability, Roles, glucido, CAGH16, Concepts, encompassing mutualism through parasitism, Metabolism Concept, RAC-3, Phenomenon, multicellular organismal biosynthetic process, ACTR, SER, single-organism biosynthetic process, posttranslational amino acid modification, Kohlenhydrate, TNRC14, LCMSMS, amino acids, Aib1, AIB1, catabolism, anabolism, 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, KAT13B, proteins, metabolic process resulting in cell growth, TNRC16, Medicago sativa subsp. sativa, Actr, DNA-dependent, potassium atom, Amplified in breast cancer-1 protein homolog, papilla, Tyr, Thyroid hormone receptor activator molecule 1, Role Concepts, biotransformation, lucerne, Catabolism, LC-MS2, incorporation, protein anabolism, symbiotic interaction between organisms, anatomical protrusion, protein biosynthetic process, wide/broad, DNA-dependent transcription, Process, Aminokarbonsaeure, external secretion, metabolism resulting in cell growth, lamina, LC-MS/MS, 2-Amino-3-(p-hydroxyphenyl)propionic acid, flanges, saccharides, Rac3, RAC3, Tyrosine, exocrine gland fluid/secretion, Steroid receptor coactivator protein 3, Role Concept, single-organism transport, shelf, protein formation, Role, secretion, Kohlenhydrat, saccharidum, PTM, Src3, SRC3, function., medium, shelves, Kalium, Class E basic helix-loop-helix protein 42, carbohidratos, projection, Sheep erythrocyte receptor, ridge, turnover, SRC-3, Amplified in breast cancer 1 protein, carbohidrato, wide, protein synthesis, spine, liquid chromatography-tandem mass spectroscopy, post-translational modification, NCoA-3, small molecule transport, Tram1, Acids, InChIKey=ZLMJMSJWJFRBEC-UHFFFAOYSA-N, glucidos, exocrine gland secretion, CBP-interacting protein, Receptor-associated coactivator 3, transcription, parasitism, exocrine gland fluid, exocrine gland fluid or secretion, lamellae, Processes, [K], Aminocarbonsaeure, bHLHe42, saccharide, alfalfa, Gene, commensalism, biosynthesis, broad, establishment of cell quiescence, Metabolic Processes, process of organ, ATP phosphohydrolase (polypeptide-unfolding), LC-MS-MS, protrusion, lamella, G1/G0 transition, Metabolism, chaperonin ATPase activity, Ensifer meliloti, LC-MSMS, symbiotic interaction between species, Gene Products, smooth ER, non-chaperonin molecular chaperone ATPase activity, transcription regulator activity, symbiosis, Metabolism Phenomena, study, symbiotic interaction between host and organism, pattern, Siglec-1, formation, distribution, nucleoplasmin ATPase activity, nutrients, peroxisome-assembly ATPase activity, Metabolic Concept, ridges, posttranslational protein modification, synthesis, Commensalism, secreted substance, bodily secretion, CTG26, Succinoglycan, Tyrosin, laminae, CD169, p|Cip, p|CIP, cellular transcription, 2.3.1.48, AIB-1, degradation, synthesize, anatomical process, Proteins, cell cycle quiescence, Phosphorylations, function, Concept, Metabolic Phenomena, polypeptide, Metabolism Concepts, LC/MS/MS, Tram-1, tirosina, Protein, Phenomena, protein biosynthesis, supply and distribution, TRAM-1, glucides, metabolism, flange, organ process, Metabolic Phenomenon, Rhizobium meliloti, mobilization, multicellular organism metabolic process, biodegradation, Metabolic, growth medium, symbiotic interaction, Mutualism, chaperonin, C9H11NO3, Understanding, Amino, Carbohydrate, post-translational amino acid modification, Protein Gene Products, host-pathogen interaction, process, processes, Gene Proteins, stationary phase, single-organism metabolic process, 2010305B15Rik, processus, liquid chromatography tandem mass spectrometry, Endosymbiosis, vesicle-fusing ATPase activity, AW321064, Anabolism2305http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320018836dbgap_ncbi~0patentfamilies~0rfam~0merops~0complex-portal~0uniprot~0wormbaseparasite~0embl-covid19~0reactome~0emdb~0wgs_masters~0ebiweb_resources~0opentargets_genetics~0biomodels_all~0ipd-mhc~0ebiweb_teams~0taxonomy~0genome_assembly~0sc-experiments~0ebiweb_people~0enzymeportal_enzymes~0ipd-nhkir~0cellosaurus~0pdbe~0chebi~0patentproteins~0interpro7~0uniref~0chembl~0pdbekb~0gpcrdb~0hgnc~0sc-genes~0intact~0rhea~0ebiweb_training~0alphafold~0imgt-hla~0patentnucleotides~0ensemblroot~0eva_studies~0non-coding~0europepmc~0pubmed~1identifiers_registry~0pdbechem~0hpa-covid19~0eva-variants-covid19~0biosamples~0gwas_catalog~0biotools~0tls_masters~0mesh~0coding~0sra~0opentargets~0efo~0embl-pathogen~0project~0pride~1human_diseases~0geo_datasets~0embl~0treefam~0uniparc~0ols~0dgva~0intenz~0go~0tsa_masters~0biosamples-covid19~0ebiweb_corporate~0omim~0lrg~0earlycause-molecular-sequences~0ipd-kir~0empiar~0rnacentral~0orcid_data_claims~0gpmdb~2lineage-covid19~0metagenomics~0pfam~0pride archive~1varsite~00Resource Reanalysis0.00.00.0070943861813695250.01.0falseSite-Specific Ser/Thr/Tyr Phosphoproteome of Sinorhizobium meliloti at Stationary Phase.Data from ProteomeXchange, PXD ID: PXD002064. File: WT2.mgf. Published as part of PLoS One. 2015 Sep 24;10(9):e0139143 . From the Abstract: {{i}} Sinorhizobium meliloti, a facultative microsymbiont of alfalfa, should fine-tune its cellular processes to live saprophytically in soils characterized with limited nutrients and diverse stresses. In this study, TiO2 enrichment and LC-MS/MS were used to uncover the site-specific Ser/Thr/Tyr phosphoproteome of S. meliloti in minimum medium at stationary phase. {{/i}}2015-10-06GPM3232001883626401955PXD002064PXD002064