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available"],"repository":["GPMDB"],"pubmed_abstract":["Gram-positive bacteria are known to export many proteins to the cell wall and growth medium, and accordingly, many studies have addressed the respective protein export mechanisms. In contrast, very little is known about the subsequent fate of these proteins. The present studies were therefore aimed at determining the fate of native exported proteins in the model organism Bacillus subtilis. Specifically, we employed a gel electrophoresis-based liquid chromatography-mass spectrometry approach to distinguish the roles of the membrane-associated quality control proteases HtrA and HtrB from those of eight other proteases that are present in the cell wall and/or growth medium of B. subtilis. Notably, HtrA and HtrB were previously shown to counteract potentially detrimental \"protein export stresses\" upon overproduction of membrane or secreted proteins. Our results show that many secreted proteins, lipoproteins, and membrane proteins of B. subtilis are potential substrates of extracytoplasmic proteases. Moreover, potentially important roles of HtrA and HtrB in the folding of native secreted proteins into a protease-resistant conformation, the liberation of lipoproteins from the membrane-cell wall interface, and the degradation of membrane proteins are uncovered. Altogether, our observations show that HtrA and HtrB are crucial for maintaining the integrity of the B. subtilis cell even under nonstress conditions."],"pubmed_title":["Extracytoplasmic proteases determining the cleavage and release of secreted proteins, lipoproteins, and membrane proteins in Bacillus subtilis."],"pubmed_authors":["Krishnappa Laxmi L,Dreisbach Annette A,Otto Andreas A,Goosens Vivianne J VJ,Cranenburgh Rocky M RM,Harwood Colin R CR,Becher Dörte D,van Dijl Jan Maarten JM,","Krishnappa Laxmi L, Dreisbach Annette A, Otto Andreas A, Goosens Vivianne J VJ, Cranenburgh Rocky M RM, Harwood Colin R CR, Becher Dörte D, van Dijl Jan Maarten JM"],"name_synonyms":["Integral Membrane Proteins, Cell Membrane, Bacillus subtilis var. natto, Bacillus natto, Circulating Lipoproteins, Lipoprotein, Surface, Proteins, Membrane-Associated, Surface Proteins, Bacillus subtilis8, Bacillus uniflagellatus., cleavage, Gene, Cell Surface, proteins, Cell Membrane Proteins, Membrane-Associated Proteins, Circulating, Integral, Membrane, Bacillus subtilis (natto), Protein Gene Products, Gene Proteins, polypeptide, Integral Membrane Protein, Vibrio subtilis, Protein, Gene Products, Membrane Proteins, Lipoproteins, Membrane Associated Proteins, Natto Bacteria, Bacillus globigii, Membrane Protein, Cell Surface Proteins, Integral Membrane"],"description_synonyms":["membrane, data, multi-cellular organism, PLXN5, body, Proteins, Liquid Chromatography, Nl1, nutrient medium, Gene, PLEXIN-B1, Mell1, whole body, ARMD7, Spectrum Analyses, membranous organ component, HtrA, HTRA, Spectrum Analysis, Cell, Bacillus uniflagellatus, SeP, Spectroscopy, polypeptide, Prss11, organism, Electrophoreses, Experiment, CEH, MMEL2, PRSS11, Protein, CT43, Gene Products, Mass, AI429470, NEPII, NL1, NL2, Analysis, SEH, growth medium., animal, Mass Spectrum Analyses, Mass Spectroscopy, Walls, SEP, Cell Walls, Mass Spectrum Analysis, Bacillus subtilis var. natto, Mass Spectrum, Wall, Bacillus natto, RSPP11, membrane of organ, CARASIL, whole organism, Analyses, medium, growth medium, FATE, Bacillus subtilis8, Spectrometry, Control, proteins, present in organism, Quality, Controls, Bacillus subtilis (natto), sEP, Protein Gene Products, Gene Proteins, Quality Controls, Vibrio subtilis, L56, Koerper, SELP, Natto Bacteria, Eph2, species, Bacillus globigii, Gram Positive Bacteria, associated, Proteomes, ORF480, NEP2"],"pubmed_title_synonyms":["Integral Membrane Proteins, Cell Membrane, Bacillus subtilis var. natto, Bacillus natto, Circulating Lipoproteins, Lipoprotein, Surface, Proteins, Membrane-Associated, Surface Proteins, Bacillus subtilis8, Bacillus uniflagellatus., cleavage, Gene, Cell Surface, proteins, Cell Membrane Proteins, Membrane-Associated Proteins, Circulating, Integral, Membrane, Bacillus subtilis (natto), Protein Gene Products, Gene Proteins, polypeptide, Integral Membrane Protein, Vibrio subtilis, Protein, Gene Products, Membrane Proteins, Lipoproteins, Membrane Associated Proteins, Natto Bacteria, Bacillus globigii, Membrane Protein, Cell Surface Proteins, Integral Membrane"],"pubmed_abstract_synonyms":["Integral Membrane Proteins, multicellular organismal catabolic process, single-organism catabolic process, multi-cellular organism, insensitive, conformation, Surface Proteins, nutrient medium, Gene, ARMD7, Membrane-Associated Proteins, Spectrum Analyses, Circulating, HtrA, HTRA, Integral, Bacillus uniflagellatus, Electrophoreses, Gene Products, Mass, Cell., Analysis, animal, Mass Spectroscopy, Walls, Cell Walls, Mass Spectrum Analysis, Cell Membrane, RSPP11, CARASIL, Circulating Lipoproteins, Analyses, FATE, catabolism, cell, Surface, Bacillus subtilis8, proteins, present in organism, Quality Controls, Vibrio subtilis, Membrane Associated Proteins, Natto Bacteria, species, Gram Positive Bacteria, associated, Membrane Protein, relational structural quality, membrane, degradation, Lipoprotein, body, Proteins, Liquid Chromatography, Cell Surface, whole body, membranous organ component, Spectrum Analysis, Cell, results, Spectroscopy, polypeptide, Prss11, organism, PRSS11, Protein, CT43, AI429470, Membrane Proteins, Mass Spectrum Analyses, Cell Surface Proteins, Bacillus subtilis var. natto, Mass Spectrum, Wall, Bacillus natto, membrane of organ, breakdown, whole organism, resistant, medium, growth medium, Membrane-Associated, Spectrometry, Control, Quality, Cell Membrane Proteins, Controls, Membrane, Bacillus subtilis (natto), Protein Gene Products, Gene Proteins, Integral Membrane Protein, L56, Koerper, Lipoproteins, Bacillus globigii, ORF480, Integral Membrane"],"view_count":["8"],"citation_count":["0"],"search_count":["5"],"full_dataset_link":["http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310004644"],"search_domains":["dbgap_ncbi~0","patentfamilies~0","rfam~0","merops~0","complex-portal~0","uniprot~0","wormbaseparasite~0","embl-covid19~0","reactome~0","emdb~0","wgs_masters~0","ebiweb_resources~0","opentargets_genetics~0","biomodels_all~0","ipd-mhc~0","ebiweb_teams~0","taxonomy~0","genome_assembly~0","sc-experiments~0","ebiweb_people~0","enzymeportal_enzymes~0","ipd-nhkir~0","cellosaurus~0","pdbe~0","chebi~0","patentproteins~0","interpro7~0","uniref~0","chembl~0","pdbekb~0","gpcrdb~0","hgnc~0","sc-genes~0","intact~0","rhea~0","ebiweb_training~0","alphafold~0","imgt-hla~0","patentnucleotides~0","ensemblroot~0","eva_studies~0","non-coding~0","europepmc~0","pubmed~1","identifiers_registry~0","pdbechem~0","hpa-covid19~0","eva-variants-covid19~0","biosamples~0","gwas_catalog~0","biotools~0","tls_masters~0","mesh~0","coding~0","sra~0","opentargets~0","efo~0","embl-pathogen~0","project~0","pride~1","human_diseases~0","geo_datasets~0","embl~0","treefam~0","uniparc~0","ols~0","dgva~0","intenz~0","go~0","tsa_masters~0","biosamples-covid19~0","ebiweb_corporate~0","omim~0","lrg~0","earlycause-molecular-sequences~0","ipd-kir~0","empiar~0","rnacentral~0","orcid_data_claims~0","gpmdb~2","lineage-covid19~0","metagenomics~0","pfam~0","pride archive~1","varsite~0"],"reanalysis_count":["0"],"submitter_keywords":["Resource Reanalysis"],"citation_count_scaled":["0.0"],"reanalysis_count_scaled":["0.0"],"view_count_scaled":["0.0024676125848241827"],"download_count_scaled":["0.0"],"normalized_connections":["1.0"],"additional_accession":[]},"is_claimable":false,"name":"Extracytoplasmic proteases determining the cleavage and release of secreted proteins, lipoproteins, and membrane proteins in Bacillus subtilis.","description":"Data from ProteomeXchange, PXD ID: PXD000078. Experiment: 100821_o2_p1_AO_AD_mut1_b, file: 100821_o2_p1_AO_AD_mut1_b_10.mzXML. Published as part of J Proteome Res. 2013 Sep 6;12(9):4101-10  . From the Abstract: {{i}} ... Gram-positive bacteria are known to export many proteins to the cell wall and growth medium, and accordingly, many studies have addressed the respective protein export mechanisms. In contrast, very little is known about the subsequent fate of these proteins. The present studies were therefore aimed at determining the fate of native exported proteins in the model organism Bacillus subtilis. Specifically, we employed a gel electrophoresis-based liquid chromatography-mass spectrometry approach to distinguish the roles of the membrane-associated quality control proteases HtrA and HtrB from those of eight other proteases that are present in the cell wall and/or growth medium of B. subtilis ... {{/i}}","dates":{"submission":"2014-10-16"},"accession":"GPM32310004644","cross_references":{"pubmed":["23937099"],"Pride":["PXD000078"],"pride":[],"Pride Archive":["PXD000078"]}}