{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/combined_protein_New.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013770_R1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013758_I3_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013774_LB1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013778_I1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013772_LB3_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013756_RSAL1_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013782_WT2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013768_R3_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013784_LB2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013764_I2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013762_RSAL2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013760_RSAL3_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013776_WT3_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013766_WT1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070479/QE_013780_R2_1.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["fabiocsn@iq.ufrj.br"],"submitter":["Proteomics Unit"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Paraburkholderia","Proteomics","Quorum sensing","Biological control.","Type vi secretion system"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070479"],"sample_protocol":["The concentrated exoproteome samples were precipitated with the addition of 4 volumes of 10% TCA in cold acetone and incubated overnight, at -30°C without rotation. Subsequently, the samples were centrifuged and the supernatant was discarded. The pellet was washed in 500 µL with 100% acetone three times and dried in a SpeedVac (Thermo Fisher Scientific, Asheville, NC, USA). The samples resuspended in 8 M urea and 2 M thiourea were digested with at a ratio of 1:50 trypsin/protein (w/w) to the solution to perform proteolysis at 35°C overnight. Peptide purification was carried out using stage-tip columns, manually packed with C18 Poros R2 resin (Applied Biosystems). The protein quantification and normalization of the samples to be injected into the mass spectrometer was performed using the Qubit® Fluorometric Quantitation (Thermo Fisher Scientific, Eugene, OR, USA). Peptides resuspended in 0.1% formic acid, were analyzed in EASY1000 nano-liquid chromatography system (Thermo Fisher Scientific, MA, USA) coupled to a Q-ExactiveTM Plus Mass spectrometer (Thermo Fisher Scientific, MA, USA). Per sample, 2 μg of peptides were loaded onto a C18 trap column (∼2 cm length, 200 μm internal diameter, 5 μm particle diameter, ReproSil-Pur C18-AQ resin, Dr. Maisch GmbH, Germany) and fractionated in a homemade C18 column (~25 cm length, 75 μm internal diameter, 3 μm particle diameter, ReproSil-Pur C18-AQ resin, Dr. Maisch GmbH, Germany). The chromatographic separation took place over 95 min with the mobile phases A (5% ACN/0.1% formic acid) and B (95% ACN/0.1% formic acid). The gradient of elution started with 7% to 25% of B for 50 min, 25% to 45 % of B for 30 min, 45% to 98% B for 7 min and keep in 98% for 8 min at a flow rate of 250 nL/min. The spectra were acquired in positive mode using data-dependent acquisition (DDA), selecting the 20 most intense precursor ions. A dynamic exclusion list of 45 s, spray voltage at 2.6 kV and capillary temperature at 250°C were employed for all analyses. The parameters for full scan were 70,000 resolution, AGC target of 3e6 ions, 100 ms maximum injection time, and the scan range of m/z 350 – 2000. The MS/MS parameters were 17,500 resolution, AGC target of 1e6 ions, 50 ms of maximum injection time, m/z 1.2 of isolation window and NCE of 30 in High-energy Collision Dissociation (HCD) cell."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The protein identification was conducted using Fragpipe v.21.1. Searches were performed against a merged file containing annotations from Paraburkholderia kururiensis (6267 entries), the reference proteome of Paraburkholderia phytofirmans downloaded from The Uniprot Consortium database (ID: UP000076852, 7,096 entries), and a list of contaminants (Frankenfield et al., 2022). MSFragger algorithm was used with a precursor mass tolerance of 10 ppm, fragment mass tolerance of 0.1 Da and trypsin as enzyme of digestion with maximun of two missed cleavages. Database search parameters included methionine oxidation (+15.9949 Da) and N-terminal acetylation (+42.0106 Da) as variable modifications, with default fixed modifications. Protein quantification was based on MS1 precursor ion intensity using the IonQuant tool. The MaxLFQ method was selected, requiring at least two ions for protein quantification. The MBR tool was applied in default mode, with a false discovery rate (FDR) controlled at < 1%. FDR were calculated using Percolator, and only high-confidence proteins were considered."],"omics_type":["Proteomics"],"labhead":["Fábio C. S. Nogueira"],"instrument_platform":[""],"labhead_affiliation":["Institute of Chemistry, Federal University of Rio de Janeiro, Brazil."],"submission_type":["PARTIAL"],"species":["Paraburkholderia Kururiensis M130"],"submitter_mail":["unidadeproteomica@gmail.com"],"publication":["10.1002/PMIC.70163"],"submitter_affiliation":["UFRJ"],"submitter_country":["Brazil"],"additional_accession":[]},"is_claimable":false,"name":"Exoproteome remodeling by the BraI/R Quorum Sensing circuit and interspecies competition in Paraburkholderia","description":"Quorum sensing (QS) is a cell-to-cell communication mechanism that enables bacteria to coordinate collective behaviors in response to population density. The BraI/R QS system is conserved among Burkholderia and Paraburkholderia species, and its regulatory role is still unknown. In this study, the BraI/R QS of P. kururiensis was investigated for biological control of another bacterial species. The results demonstrate that the functional BraI/R system influences interbacterial competition, as braI and braR mutant strains failed to inhibit the growth of Escherichia coli, in contrast to the wild-type strain. These findings suggest that the BraI/R QS system plays a regulatory role in modulating interspecies antagonism. Comparative exoproteome analyses were performed for the wild-type and the BraI/R QS-mutant P. kururiensis strains, revealing distinct protein populations, including structural and effector proteins of the Type VI secretion system (T6SS). Genomic mapping revealed that two of those T6SS-proteins were encoded within a specific T6SS gene cluster (T6SS-3), while others originate outside any major T6SS gene cluster. The identification of exoproteome targets regulated by the BraI/R QS system represents a significant advance toward the understanding of the molecular mechanisms underpinning P. kururiensis interactions with competing bacteria, further supporting its potential as a biological control agent against phytopathogenic and/or free-living 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