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Analysis of proteins from cytoplasmic, inner membrane, periplasmic, and outer membrane fractions yielded coverage of 25% of the theoretical proteome. Confident subcellular location could be assigned to over 1000 proteins, with good agreement between experimentally observed location and predicted/known protein properties. Comparison of protein location under the different environmental conditions provided insight into dynamic protein localization and possible moonlighting (multiple function) activities. Notable examples of dynamic localization were the response regulators of two-component regulatory systems (e.g., ArcB and PhoQ). The DNA-binding protein Dps that is generally regarded as cytoplasmic was significantly enriched in the outer membrane for all growth conditions examined, suggestive of moonlighting activities. These observations imply the existence of unknown transport mechanisms and novel functions for a subset of Salmonella proteins. Overall, this work provides a catalog of experimentally verified subcellular protein locations for Salmonella and a framework for further investigations using computational modeling."],"pubmed_title":["A Comprehensive Subcellular Proteomic Survey of Salmonella Grown under Phagosome-Mimicking versus Standard Laboratory Conditions."],"pubmed_authors":["Brown Roslyn N RN,Sanford James A JA,Park Jea H JH,Deatherage Brooke L BL,Champion Boyd L BL,Smith Richard D RD,Heffron Fred F,Adkins Joshua N JN,","Brown Roslyn N RN, Sanford James A JA, Park Jea H JH, Deatherage Brooke L BL, Champion Boyd L BL, Smith Richard D RD, Heffron Fred F, Adkins Joshua N JN"],"name_synonyms":["phagosome, Samonella, Laboratory."],"description_synonyms":["Gpi, membrane, data, determination, AI461847, Laboratory, Salmonella cholerae-suis, Proteins, Gene, MF, membranous organ component, Amf, predicted, polypeptide, Readability, mOC-X, chemical analysis, Protein, proteomic analysis, Gene Products, Pgi, NK|GPI, relational spatial quality, Gpi-1, phagosome, placement, NK, Org, ORG, membrane of organ, Gpi-1r, Nlk, Gpi-1s, Phi, Bacillus cholerae-suis, Gpi-1t, Gpi1-r, Gpi1-s, Salmonella choleraesuis, proteins, Understanding, Gpi1-t, Protein Gene Products, Gene Proteins, proteins., assay, location, Proteomes, Bglap-rs1, Salmonella enterica ser. choleraesuis, Gpi1s"],"pubmed_title_synonyms":["phagosome, Samonella, Laboratory."],"pubmed_abstract_synonyms":["establishment and maintenance of substance location, membrane, DNS, determination, (Deoxyribonucleotide)n, Samonella, Laboratory, DNAn+1, Salmonella cholerae-suis, Proteins, Gene, function, Double-Stranded, membranous organ component, predicted, Deoxyribonucleic acids, (Deoxyribonucleotide)n+m, polypeptide, solute:solute exchange, Readability, single organism localization, Deoxyribonucleic Acid, single-organism transport, responsivity, chemical analysis, Protein, proteomic analysis, Gene Products, establishment and maintenance of position, establishment and maintenance of localization, relational spatial quality, establishment and maintenance of substrate location, ds-DNA, phagosome, desoxyribose nucleic acid, placement, reactivity, asymmetric protein localization, thymus nucleic acid, membrane of organ, DPS, growth pattern, non-developmental growth, ligand, Bacillus cholerae-suis, deoxyribonucleic acid, Double Stranded, Salmonella choleraesuis, proteins, single-organism localization, W, Understanding, Samonella., Protein Gene Products, Gene Proteins, dps, localisation, ds DNA, Desoxyribonukleinsaeure, small molecule transport, asymmetric protein localisation, Double-Stranded DNA, assay, (Deoxyribonucleotide)m, response, DNA, deoxyribonucleic acids, establishment and maintenance of protein localization, DNAn, establishment and maintenance of asymmetric protein localization, location, protein localisation, Proteomes, Salmonella enterica ser. choleraesuis, establishment and maintenance of cellular component location"],"view_count":["10"],"citation_count":["0"],"search_count":["3"],"full_dataset_link":["http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310003265"],"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","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","varsite~0"],"citation_count_scaled":["0.0"],"reanalysis_count_scaled":["0.0"],"view_count_scaled":["0.0030845157310302285"],"download_count_scaled":["0.0"],"reanalysis_count":["0"],"normalized_connections":["1.0"],"additional_accession":[]},"is_claimable":false,"name":"A Comprehensive Subcellular Proteomic Survey of Salmonella Grown under Phagosome-Mimicking versus Standard Laboratory Conditions.","description":"Data from PeptideAtlas, [[http://www.peptideatlas.org/PASS/PASS00551 PASS00551]]. File: SBEP_STM_subcell-53c_14Jan11_Doc_10-09-53.mzml. Published as part of  . From the Abstract: {{i}} Towards developing a systems-level pathobiological understanding of Salmonella enterica, we performed a subcellular proteomic analysis of this pathogen grown under standard laboratory and phagosome-mimicking conditions in vitro. Analysis of proteins from cytoplasmic, inner membrane, periplasmic, and outer membrane fractions yielded coverage of 25% of the theoretical proteome. Confident subcellular location could be assigned to over 1000 proteins, with good agreement between experimentally observed location and predicted/known protein properties. {{/i}}","dates":{"submission":"2014-08-20"},"accession":"GPM32310003265","cross_references":{"pubmed":["22900174"]}}