{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077803/KEY_Kotsakis.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077803/dependentPeptides.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077803/proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077803/modificationSpecificPeptides.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077803/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077803/peptides.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077803/DDA_18717.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077803/DDA_18718.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077803/DDA_18719.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["skotsakis@pasteur.gr"],"submitter":["Martina Samiotaki"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Myx-2","Myx-1","Myxobacteria"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077803"],"sample_protocol":["Purified MYX-1and MYX-2 were suspended in a buffer containing 4% SDS and 0.1 M dithiothreitol (DTT) in 0.1 M TEAB and processed according to the single-pot, solid-phase-enhanced sample preparation Sp3-mediated protein digestion protocol (108) including an alkylation step in 10 mg/ml iodoacetamide. Proteins were captured on magnetic beads (1:1 mixture of hydrophilic and hydrophobic SpeedBead Magnetic Carboxylate, Cytiva) at the presence of 50% ethanol. The beads were washed two times with 80% ethanol and once with 100% acetonitrile. Digestion was carried out using 0.5 μg Trypsin/LysC (MS grade, Promega) at 37 oC.  The isolated peptides were analyzed with a liquid chromatography tandem mass spectrometry (LC-MS/MS) setup consisting of a Dionex Ultimate 3000 nano RSLC online with a Thermo Q Exactive HF-X Orbitrap mass spectrometer. Samples were directly injected and separated on an 25 cm-long analytical C18 column (PepSep, 1.9 μm beads, 75 µm ID) starting with a gradient of 7% buffer D (0.1% Formic acid in 80% acetonitrile) to 35% for 40 min and followed by an increase to 45% in 5 min and a second increase to 99% in 0.5 min and then kept constant for equilibration for 14.5 min. MS data were acquired in a data-dependent (DDA) strategy selecting up to top 12 precursors based on precursor abundance in the survey scan (m/z 350–1500). The resolution of the survey scan was 120,000 (at m/z 200) with a target value of 3∙106 ions and a maximum injection time of 100 ms. HCD MS/MS spectra were acquired with a target value of 105  and resolution of 15,000 (at m/z 200) using an NCE of 28. The maximum injection time for MS/MS was 22 ms. Dynamic exclusion was enabled for 30 s after one MS/MS spectra acquisition. Peptide match was set as preferred. The isolation window for MS/MS fragmentation was set to 1.2 m/z. A lock mass of m/z 445.12003 was used throughout the analysis."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The obtained data were searched using the MaxQuant Software v2.1.4.0 (109) using Andromeda, against the MYX-1 and MYX-2 sequences with the MaxQuant common contaminant database. To be accepted for the identification, an error of less than 20 ppm (first recalibration search) and 4.5 ppm tolerance in the main search of peptide mass tolerance was accepted. Up to 2 missed cleavages were allowed and the modifications taken into account were: Oxidation (M); Acetyl (Protein N-term); Deamidation (NQ) as variable modifications and Carbamidomethylation (Cys) as fixed modifications. Tryptic semi-specific search was used. Matching between runs and second peptide options were activated. Protein, peptide and “site” identifications were validated at a FDR of 1% using a reversed database. The label minimum ratio count was set to 2. In order to find unknown modifications, the dependent peptide search was activated."],"omics_type":["Proteomics"],"labhead":["Stathis D. Kotsakis"],"instrument_platform":[""],"labhead_affiliation":["Laboratory of Bacteriology, Hellenic Pasteur Institute, Athens, Greece"],"submission_type":["PARTIAL"],"species":["Myxococcales"],"submitter_mail":["samiotaki@fleming.gr"],"publication":["Not available"],"submitter_affiliation":["Protein Analysis Laboratory\nB.S.R.C. \"Alexander Fleming\",\nAlexander Fleming Street 34\n16672, Vari,\nGreece"],"submitter_country":["Greece"],"additional_accession":[]},"is_claimable":false,"name":"Myxobacterial metallo-β-lactamases","description":"Understanding the biology of B1 metallo-β-lactamases (MβLs) in their native hosts and the molecular bases of the adaptive mechanisms during the transfer process to human pathogens, may provide novel therapeutic insights against these important resistance factors. Through large scale phylogenomic analyses, we identified Bacteroidota and Myxococcota as the primary hosts of the enzymes in environmental habitats. The monophyletic lineage of MβL homologues from the predatory members of the latter phylum shared common ancestry with clinically relevant families found in γ-Proteobacteria, highlighting their evolutionary significance. Resistance phenotypes and biochemical properties of native MβLs from three myxobacterial genera expressed in the model γ-proteobacterium, Escherichia coli, and comparisons with the New Delhi Metallo-β-lactamase revealed that evolution of the enzymes concerned mainly adaptations enhancing their production in the new hosts rather than functional differentiation. Periplasmic localization is the main evolved trait, with E. coli not recognizing optimally the signal peptides of the environmental MβLs which were secreted as soluble proteins in the cell envelope despite predicted to be lipoproteins. The unique features of N-terminal secretory signals of myxobacterial MβLs likely reflected the enzymes integration into the physiology of their hosts and pointed to naturally occurring molecules potentially controlling their 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