{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/sample_file_Rhodococcus_erythropolis_X5.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/TMT-channel.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20230309-1707_LUM2_1005940_FKJ_VG_Rh_erythropolis_X5_4C2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20230309-1718_LUM2_1005941_FKJ_VG_Rh_erythropolis_X5_4C3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20211024-1316_QEHF3_1000469_FKJ_JB_lfq_bacteria_24.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20211024-0522_QEHF3_1000463_FKJ_JB_lfq_bacteria_19.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20230309-1803_LUM2_1005945_FKJ_VG_Rh_erythropolis_X5_24C3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20211024-1018_QEHF3_1000467_FKJ_JB_lfq_bacteria_22.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20211024-1604_QEHF3_1000471_FKJ_JB_lfq_bacteria_25.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20230309-1656_LUM2_1005939_FKJ_VG_Rh_erythropolis_X5_4C1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20211024-0820_QEHF3_1000465_FKJ_JB_lfq_bacteria_21.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20211024-1147_QEHF3_1000468_FKJ_JB_lfq_bacteria_23.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20211024-1823_QEHF3_1000472_FKJ_JB_lfq_bacteria_26.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20211024-0651_QEHF3_1000464_FKJ_JB_lfq_bacteria_20.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20230309-1741_LUM2_1005943_FKJ_VG_Rh_erythropolis_X5_24C1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050807/20230309-1752_LUM2_1005944_FKJ_VG_Rh_erythropolis_X5_24C2.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["iatarasova@yandex.ru"],"submitter":["Tomiris Kusainova"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Directms1","Rhodococcus erythropolis x5","Lfq","Proteomics","Tmt"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD050807"],"sample_protocol":["R. erythropolis X5 cells were grown in an orbital shaking incubator at 180 rpm at two different temperatures (28°С and 6°С) for 3 and 11 days, respectively, with three biological replicates. The cultivation was carried out in 750 mL Erlenmeyer flasks with 100 mL of the modified Evans mineral salts medium supplemented with 2 mL of n-hexadecane. The composition of the cultivation medium was as follows (per liter): K2HPO4, 8.71 g; 5 M solution of NH4Cl, 1 mL; 0.1 M solution of Na2SO4, 1 mL; 62 mM solution of MgCl2, 1 mL; 1 mM solution of CaCl2, 1 mL; 0.005 mM solution of (NH4)6Mo7O24, 1 mL; trace element solution, 1 mL. The value of рН was adjusted to 7.5 by concentrated HCl. Composition of the trace element solution in 1% water solution of HCl (g/L): ZnO, 0.41 g; FeCl3, 2.9 g; MnCl2, 1.28 g; CuCl2, 0.13 g; CoCl2, 0.26 g; H3BO3, 0.06 g. Cell pellets were resuspended in 200 µL lysis buffer ( 50mM ABC, 10% ACN, 0.1% ProteaseMAX™ Surfactant — Trypsin Enhancer). Cells incubated for 45 min  at room temperature, after that they were boiled for 10 min at 95 °C, and then cooled down on ice. To lyse cells, the samples were sonicated for 5 min (1 sec on 1 sec off) on 60 % amplitude (QSonica Q125, Newtown, Connecticut, USA). Samples were centrifuged for 5 min on 10 000 g, then supernatant was taken, and protein concentration was measured by BCA kit (Thermo Scientific, Germany). DTT 10mM was added for 20 min at 56 °C, followed by incubation with IAA for 30 min in the dark at room temperature.  Lys-c was added in 1:100 m/m ratio and samples incubated for 2h at 37 °C then trypsin was added in 1:50 m/m ratio and samples incubated overnight at 37 °C. Digest was stopped by adding 1 % TFA, then samples were desalted with OASIS HLB cartridges (Waters, USA) and dried in a vacuum concentrator. The LC-MS experiment was performed using Orbitrap Q Exactive HF mass spectrometer (Thermo Scientific, San Jose, CA, USA) coupled to Dionex UltiMate 3000 LC system (Thermo Fisher Scientific, Germering, Germany. Trap column μ-Precolumn C18 PepMap100 (5 μm, 300 μm, i.d. 5 mm, 100 Å) (Thermo Fisher Scientific, USA) and self-packed analytical column (Reprosil-Pur 3 μm, 75 μm i.d., 15 cm length) were employed for separation. Mobile phases were as follows: (A) 0.1% formic acid (FA) in water; (B) 95% ACN, 0.1% FA in water. The gradient was from 5% to 35% phase B in 4.8 min at 1.5 μL/min. Total method time including column washing and equilibration was 7.5 min. Field asymmetric ion mobility spectrometry (FAIMS) separations were performed with the following compensation voltages (CV) -50 V, -65 V, and -80 V in a stepwise mode during LC-MS analysis. Data acquisition was performed in MS1-only mode. Full MS scans were acquired in a range from m/z 375 to 1500 at a resolution of 120,000 at m/z 200 with AGC target of 4e6, 1 microscan, and 50 ms maximum injection time. Samples were resuspended in phase A and quantities of 1 \uD835\uDF07g were loaded per injection. MS/MS-based analysis of samples was performed using Orbitrap Q Exactive HF mass spectrometer (Thermo Fisher Scientific, San Jose, CA, USA) coupled to UltiMate 3000 LC system. Trap column µ-Precolumn C18 PepMap100 (5 µm, 300 µm, i.d. 5 mm, 100 Å) (Thermo Fisher Scientific, USA) and self-packed analytical column (Inertsil 2 µm, 75 µm i.d., 25 cm length) were employed for separation. Mobile phases were as follows: (A) 0.1 % FA in water; (B) 95 % ACN, 0.1 % FA in water. For TMT-based quantitation, the gradient from 2% to 30% phase B for 114 min at a flow rate of 300 nL/min was used. Data was acquired in top20 mode. Full MS scans were acquired in a range from m/z 300 to 1400 at a resolution of 60000 at m/z 200 with AGC (Automatic Gain Control) target of 3e6, 1 microscan, and 50 ms maximum injection time. Precursor ions were isolated in a 1.4 m/z window and accumulated for a maximum of 100 ms or until the 1e5 AGC target was reached. For label free quantitation, the gradient from 2% to 40% phase B for 60 min at a flow rate of 300 nL/min was used. Full MS scans were acquired in a range from m/z 300 to 1400 at a resolution of 60000 at m/z 200 with AGC target of 3e6, 1 microscan, and 50 ms maximum injection time. Precursor ions were isolated in a 1.4 m/z window and accumulated for a maximum of 50 ms or until the AGC target of 1e5 charges was reached. Precursors of charge states from 2+ to 6+ (inclusive) were scheduled for fragmentation."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Thermo raw files were converted to mzML format using ThermoRawFileParser (https://github.com/compomics/ThermoRawFileParser). Peptide feature deteсtion was performed using the Biosaur2 software. For MS1 data the proteomic search engine ms1searchpy was used for protein identification. For MS2 data the proteomic search engine Identipy (https://github.com/levitsky/identipy) was used for protein identification search. Post-search validation done with Scavager tool (https://github.com/markmipt/scavager). Search was performed against the SwissProt + TrEMBL database (accessed on 06 Dec 2020) of bacterial proteins and strain-specific databases based on annotations of bacterial genomes. . Mass tolerance for precursors in all data was ±10 ppm, fragment mass tolerance for DDA data was 0.01 Da. Carbamidomethylation of cysteine residues was fixed modification, no variable modifications and no missed cleavages were allowed in MS1 search. For DDA data, the variable methionine oxidation and tmt10plex tags (where applicable) were allowed.  The other search parameters were used by default. Protein identifications were filtered to 1% FDR using the target-decoy approach. Quantification was performed using Diffacto."],"omics_type":["Proteomics"],"labhead":["Dr Irina A. Tarasova"],"instrument_platform":[""],"labhead_affiliation":["INEPCP FRCCP RAS, Moscow, Russia"],"submission_type":["PARTIAL"],"species":["Rhodococcus Erythropolis"],"submitter_mail":["kusainova7531@gmail.com"],"publication":["10.1093/FEMSML/UQAG027"],"submitter_affiliation":["V. L. Talrose Institute for Energy Problems of Chemical Physics, N. N. Semenov Federal Research Center for Chemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia\n\nMoscow Institute of Physics and Technology, 141701 Dolgoprudny, Russia"],"submitter_country":["Russia"],"additional_accession":[]},"is_claimable":false,"name":"Quantitative assessment of microbiomes using ultra-fast MS/MS-free metaproteomics: Rhodococcus erythropolis X5","description":"This study presents an adaptation of the novel ultrafast MS1-based method called DirectMS1 to characterization of the single microorganisms and microbiomes. Using DirectMS1 we demonstrate the blind  identification (with no prior knowledge of the bacterias in the sample) of a single bacterial species and microbial compositions using two-step database search against the microbial part of SwissProt and TrEMBL (62Gb database size), the evaluation of fold changes in biomass of microorganisms between the metaproteomic samples, and the assessment of metabolic activity of Rhodococcus species responding to a change in growth conditions and cold 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