{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_7G2.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_WT3.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_7G3.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_WT2.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_7G1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_WT1.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_WT1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_7G3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_7G1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_WT3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_7G2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077370/YM_WT2.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["swhan@cau.ac.kr"],"submitter":["Sang-Wook Han"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Acidovorax citrulli","Lc-ms/ms","Polytopic transmembrane protein"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077370"],"tissue":["Cell Culture"],"sample_protocol":["For proteomic analysis, Ac and ptmAc:Tn5 were used, and a label-free shotgun comparative proteomic approach was carried out using a previously reported protocol (Park et al., 2020b). Briefly, Ac strains were grown in TSB and harvested at an OD600 of 0.5 by centrifugation. The harvested cells were disrupted by an Ultrasonic Processor (Colo Parmer, Vernon Hills, IL, USA). Total proteins were concentrated using trichloroacetic acid (TCA) precipitation and digested by trypsin. After cleaning the tryptic-digested proteins using the Sep-Pak Vac 1cc tC18 cartridge (Waters, Milford, MA, USA), peptide concentration was determined using a BCA assay kit (Thermo Fisher Scientific, Waltham, MA, USA). One μg of each sample (two strains with three biological replicates) was injected into a split-free nano LC (EASY-nLC II; Thermo Fisher Scientific, Bremen, Germany) combined with an LTQ Velos Pro instrument (Thermo Fisher Scientific) by the nanospray ion mode. Tryptic-digested peptides were loaded onto a 7.5 cm of MAGIC C18AQ 200A (5 µm) (Michrom BioResources, Auburn, CA, USA) with 300 nL/min flow rate for 420 min under water/acetonitrile gradient using buffer A (water with 0.1% formic acid) buffer B (100% acetonitrile with 0.1% formic acid). For the mass spectra, six of data-dependent MS/MS scans with m/z 300-2000 range of mass were used. Dynamic exclusion was allowed under one repeat, 0.5 min duration, and 3 min exclusion. The ion charge state selection was permitted for 2+ and 3+. From the full mass scan, six of the most intense ions were chosen."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["- Mass spectrometry analysis A total of 6 biological samples, including three biological replicates, were analyzed by LC-MS/MS. Each sample (2 µg) was analyzed on a split-free nano LC device (EASY-nLC II; Thermo Fisher Scientific, Bremen, Germany) connected to an LTQ Velos Pro instrument (Thermo Fisher Scientific, Bremen, Germany) via the nanospray ion mode. The digested samples were separated by a column packed in-house with 7.5 cm of MAGIC C18AQ 200A (5 µm) material (Michrom BioResources, Auburn, CA, USA). The peptides were eluted at a flow rate of 300 nL/min, using a 420 min water/ACN gradient (Solvent A, water with 0.1% formic acid; Solvent B, 100% ACN with 0.1% formic acid) as follows: 5 min 7% B, 380 min gradient to 35% B, and 10 min to 80% B, with a final hold at 7% B for 25 min. Full mass spectra were acquired in six data-dependent MS/MS scans over a mass range of m/z 300–2000. Dynamic exclusion was allowed with a repeat count of 1, repeat duration of 0.5 min, and exclusion duration of 3.0 min, with charge state selection enabled to preferentially select 2+ and 3+ ions. Peptides were transferred with a 1.8 kV spray voltage and a desolvation capillary temperature of 200 °C. Up to six of the most intense ions in each full MS scan were consecutively collected for fragmentation and examined in centroid mode within the linear ion trap part of the instrument.  - Protein/peptide identification Thermo Proteome Discoverer 1.3 (ver. 1.3.0.399) with the SEQUEST search algorithm was used for interpretation of acquired MS/MS spectra. The spectra were searched against Acidovorax citrulli strain KACC17005 databases from the National Center for Biotechnology Information. A target-decoy search was employed to enhance the confidence of correct identification. Trypsin was set as the enzyme, and two missed cleavages were permitted. All accepted Acidovorax citrulli eptides had a false discovery rate of 0.01 with reversed database searches, and precursor mass accuracies of 100 ppm. In addition, the probability scores of all peptides were over 20. The oxidation of methionine was fixed as a possible modification. Proteins that matched at least two unique peptides were considered to be present in the sample. Then, the identified proteins were re-imported into Scaffold 4 (Proteome software, Portland, OR, USA) for visualization and comparison of the proteomics data. After removing decoy proteins, peptide spectrum match (PSM) was used for comparative analysis. PSMs from each protein were normalized against the total PSMs from all proteins in a sample. Proteins shared among the three biological replicates were used for comparison. The average of normalized PSMs in the three biological replicates was calculated per protein and used as a comparison value to identify differentially (over 2-fold) expressed proteins."],"omics_type":["Proteomics"],"labhead":["Sang-Wook Han"],"instrument_platform":[""],"labhead_affiliation":["Department of Plant Science and Technology, Chung-Ang University, Anseong 17546, Republic of Korea"],"submission_type":["PARTIAL"],"species":["Paracidovorax"],"submitter_mail":["swhan@cau.ac.kr"],"publication":["Not available"],"submitter_affiliation":["Chung-Ang University"],"submitter_country":["South Korea"],"additional_accession":[]},"is_claimable":false,"name":"Comparative proteomic analysis for a polytopic transmembrane protein in Acidovorax citrulli","description":"- Identification of proteins whose expression was affected by a polytopic transmembrane protein in Acidovorax citrulli str. KACC17005 - Shotgun proteomic analysis was used -  Two strains were used with three biological replicates (total 6 samples). YM_WT: the wild-type strain. YM_7G: a polytopic transmembrane protein knockout 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