{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,29]],"date-time":"2025-12-29T11:10:11Z","timestamp":1767006611965,"version":"3.41.2"},"reference-count":159,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2021,4,9]],"date-time":"2021-04-09T00:00:00Z","timestamp":1617926400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Bioinform."],"abstract":"<jats:p>OMPdb (<jats:ext-link>www.ompdb.org<\/jats:ext-link>) was introduced as a database for \u03b2-barrel outer membrane proteins from Gram-negative bacteria in 2011 and then included 69,354 entries classified into 85 families. The database has been updated continuously using a collection of characteristic profile Hidden Markov Models able to discriminate between the different families of prokaryotic transmembrane \u03b2-barrels. The number of families has increased ultimately to a total of 129 families in the current, second major version of OMPdb. New additions have been made in parallel with efforts to update existing families and add novel families. Here, we present the upgrade of OMPdb, which from now on aims to become a global repository for all transmembrane \u03b2-barrel proteins, both eukaryotic and bacterial.<\/jats:p>","DOI":"10.3389\/fbinf.2021.646581","type":"journal-article","created":{"date-parts":[[2021,4,9]],"date-time":"2021-04-09T06:54:47Z","timestamp":1617951287000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":13,"title":["OMPdb: A Global Hub of Beta-Barrel Outer Membrane Proteins"],"prefix":"10.3389","volume":"1","author":[{"given":"Ahmed F.","family":"Roumia","sequence":"first","affiliation":[]},{"given":"Konstantinos D.","family":"Tsirigos","sequence":"additional","affiliation":[]},{"given":"Margarita C.","family":"Theodoropoulou","sequence":"additional","affiliation":[]},{"given":"Ioannis A.","family":"Tamposis","sequence":"additional","affiliation":[]},{"given":"Stavros J.","family":"Hamodrakas","sequence":"additional","affiliation":[]},{"given":"Pantelis G.","family":"Bagos","sequence":"additional","affiliation":[]}],"member":"1965","published-online":{"date-parts":[[2021,4,9]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1111\/j.1574-6968.2001.tb10642.x","article-title":"Multiple facets of bacterial porins","volume":"199","author":"Achouak","year":"2006","journal-title":"FEMS Microbiol. Lett."},{"key":"B2","doi-asserted-by":"publisher","first-page":"420","DOI":"10.1038\/s41587-019-0036-z","article-title":"SignalP 5.0 improves signal peptide predictions using deep neural networks","volume":"37","author":"Almagro Armenteros","year":"2019","journal-title":"Nat. Biotechnol."},{"key":"B3","doi-asserted-by":"publisher","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: a new generation of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"B4","doi-asserted-by":"publisher","first-page":"482","DOI":"10.1016\/j.tibs.2008.07.004","article-title":"Disparate proteins use similar architectures to damage membranes","volume":"33","author":"Anderluh","year":"2008","journal-title":"Trends Biochem. Sci."},{"key":"B5","doi-asserted-by":"publisher","first-page":"bav063","DOI":"10.1093\/database\/bav063","article-title":"Creating a specialist protein resource network: a meeting report for the protein bioinformatics and community resources retreat","volume":"2015","author":"Babbitt","year":"2015","journal-title":"Database"},{"key":"B6","doi-asserted-by":"publisher","first-page":"W400","DOI":"10.1093\/nar\/gkh417","article-title":"PRED-TMBB: a web server for predicting the topology of \u03b2-barrel outer membrane proteins","volume":"32","author":"Bagos","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"B7","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1146\/annurev.micro.60.080805.142106","article-title":"Curli biogenesis and function","volume":"60","author":"Barnhart","year":"2006","journal-title":"Annu. Rev. Microbiol."},{"key":"B8","doi-asserted-by":"publisher","first-page":"15370","DOI":"10.1073\/pnas.0808115105","article-title":"Structure of the human voltage-dependent anion channel","volume":"105","author":"Bayrhuber","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"B9","doi-asserted-by":"publisher","first-page":"431","DOI":"10.1007\/s10532-009-9313-8","article-title":"A beta-barrel outer membrane protein facilitates cellular uptake of polychlorophenols in Cupriavidus necator","volume":"21","author":"Belchik","year":"2010","journal-title":"Biodegradation"},{"key":"B10","doi-asserted-by":"publisher","first-page":"1763","DOI":"10.1128\/JB.06711-11","article-title":"Mutational analyses reveal overall topology and functional regions of NilB, a bacterial outer membrane protein required for host association in a model of animal-microbe mutualism","volume":"194","author":"Bhasin","year":"2012","journal-title":"J. Bacteriol."},{"key":"B11","doi-asserted-by":"publisher","first-page":"W252","DOI":"10.1093\/nar\/gku340","article-title":"SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information","volume":"42","author":"Biasini","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"B12","doi-asserted-by":"publisher","first-page":"1881","DOI":"10.1016\/j.bbamem.2007.07.021","article-title":"Structural biology of membrane-intrinsic \u03b2-barrel enzymes: Sentinels of the bacterial outer membrane","volume":"1778","author":"Bishop","year":"2008","journal-title":"Biochim. Biophys. Acta - Biomembr."},{"key":"B13","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1111\/j.1574-6976.1995.tb00177.x","article-title":"Energy-coupled transport and signal transduction through the Gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins","volume":"16","author":"Braun","year":"1995","journal-title":"FEMS Microbiol. Rev."},{"key":"B14","doi-asserted-by":"publisher","first-page":"E5439","DOI":"10.1073\/pnas.1411942111","article-title":"Structure of the nonameric bacterial amyloid secretion channel","volume":"111","author":"Cao","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B15","doi-asserted-by":"publisher","first-page":"1158","DOI":"10.1110\/ps.0223603","article-title":"Fishing new proteins in the twilight zone of genomes: the test case of outer membrane proteins in Escherichia coli K12, Escherichia coli O157:H7, and other Gram-negative bacteria","volume":"12","author":"Casadio","year":"2003","journal-title":"Protein Sci."},{"key":"B16","doi-asserted-by":"publisher","first-page":"174","DOI":"10.1016\/S1360-1385(00)01598-3","article-title":"Membrane heredity and early chloroplast evolution","volume":"5","author":"Cavalier-Smith","year":"2000","journal-title":"Trends Plant Sci."},{"key":"B17","unstructured":"The complement system and innate immunity5982\n            Charles A JanewayJ.\n            TraversP.\n            WalportM.\n            ShlomchikM. J.\n          \n            GibbsS.\n          New York, NYGarland ScienceImmunobiology Interactive2001"},{"key":"B18","doi-asserted-by":"publisher","first-page":"953","DOI":"10.3389\/fmicb.2019.00953","article-title":"Distinct roles of outer membrane porins in antibiotic resistance and membrane integrity in Escherichia coli","volume":"10","author":"Choi","year":"2019","journal-title":"Front. Microbiol."},{"key":"B19","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1016\/j.bbrc.2007.03.162","article-title":"Signal-CF: a subsite-coupled and window-fusing approach for predicting signal peptides","volume":"357","author":"Chou","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"B20","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1201\/b14028-32","article-title":"Mycoplasmas","volume-title":"Laboratory Diagnosis of Bacterial Infections","author":"Cimolai","year":"2001"},{"key":"B21","doi-asserted-by":"publisher","first-page":"39750","DOI":"10.1074\/jbc.M405971200","article-title":"Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 \u00c5 resolution","volume":"279","author":"Collins","year":"2004","journal-title":"J. Biol. Chem."},{"key":"B22","unstructured":"Microfouling: the role of primary film forming marine bacteria598609\n            CorpeW. A.\n          ci.nii.ac.jp1972"},{"key":"B23","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1128\/JB.165.1.181-192.1986","article-title":"Protein fusions of \u03b2-galactosidase to the ferrichrome-iron receptor of Escherichia coli K-12","volume":"165","author":"Coulton","year":"1986","journal-title":"J. Bacteriol."},{"key":"B24","doi-asserted-by":"publisher","first-page":"5178","DOI":"10.1128\/IAI.00834-10","article-title":"Surface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum","volume":"78","author":"Cox","year":"2010","journal-title":"Infect. Immun."},{"key":"B25","unstructured":"Biomedical polymers: bacterial adhesion, colonization and infection219301\n            DankertJ.\n            HogtA. H.\n            FeijenJ.\n          ci.nii.ac.jp21986"},{"key":"B26","doi-asserted-by":"publisher","first-page":"1541","DOI":"10.1128\/CVI.00141-08","article-title":"Immunomagnetic separation and coagglutination of Vibrio parahaemolyticus with anti-flagellar protein monoclonal antibody","volume":"15","author":"Datta","year":"2008","journal-title":"Clin. Vaccine Immunol."},{"key":"B27","doi-asserted-by":"publisher","first-page":"1845","DOI":"10.1105\/tpc.19.00001","article-title":"Chloroplast outer membrane \u03b2-Barrel proteins use components of the general import apparatus","volume":"31","author":"Day","year":"2019","journal-title":"Plant Cell"},{"key":"B28","doi-asserted-by":"publisher","first-page":"1793","DOI":"10.1016\/j.febslet.2010.02.049","article-title":"Voltage-dependent anion-selective channel (VDAC) in the plasma membrane","volume":"584","author":"De Pinto","year":"2010","journal-title":"FEBS Lett."},{"key":"B29","doi-asserted-by":"publisher","first-page":"7385","DOI":"10.1073\/pnas.1017442108","article-title":"Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins","volume":"108","author":"De","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B30","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1016\/j.bbamcr.2004.05.001","article-title":"Type I secretion in gram-negative bacteria","volume":"1694","author":"Delepelaire","year":"2004","journal-title":"Biochim. Biophys. Acta - Mol. Cell Res."},{"key":"B31","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1016\/j.resmic.2003.10.002","article-title":"The autotransporter secretion system","volume":"155","author":"Desvaux","year":"2004","journal-title":"Res. Microbiol."},{"key":"B32","doi-asserted-by":"publisher","first-page":"549","DOI":"10.1016\/S0021-9258(19)57427-0","article-title":"The structure of human complement component C7 and the C5b-7 complex","volume":"263","author":"DiScipio","year":"1988","journal-title":"J. Biol. Chem."},{"key":"B33","doi-asserted-by":"publisher","first-page":"D283","DOI":"10.1093\/nar\/gku1119","article-title":"Expediting topology data gathering for the TOPDB database","volume":"43","author":"Dobson","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"B34","doi-asserted-by":"publisher","first-page":"52","DOI":"10.1038\/nature13464","article-title":"Structural basis for outer membrane lipopolysaccharide insertion","volume":"511","author":"Dong","year":"2014","journal-title":"Nature"},{"key":"B35","doi-asserted-by":"publisher","first-page":"10588","DOI":"10.1038\/ncomms10588","article-title":"Structure of the poly-C9 component of the complement membrane attack complex","volume":"4","author":"Dudkina","year":"2016","journal-title":"Nat. Commun."},{"key":"B36","doi-asserted-by":"publisher","first-page":"755","DOI":"10.1093\/bioinformatics\/14.9.755","article-title":"Profile hidden Markov models","volume":"14","author":"Eddy","year":"1998","journal-title":"Bioinformatics"},{"key":"B37","doi-asserted-by":"publisher","first-page":"1792","DOI":"10.1093\/nar\/gkh340","article-title":"MUSCLE: multiple sequence alignment with high accuracy and high throughput","volume":"32","author":"Edgar","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"B38","doi-asserted-by":"publisher","first-page":"39211","DOI":"10.1074\/jbc.M111.280933","article-title":"Structural basis for the interaction of lipopolysaccharide with outer membrane protein H (OprH) from Pseudomonas aeruginosa","volume":"286","author":"Edrington","year":"2011","journal-title":"J. Biol. Chem."},{"key":"B39","doi-asserted-by":"publisher","first-page":"665","DOI":"10.1016\/j.cell.2020.03.032","article-title":"The crystal structure of a biological insulated transmembrane molecular wire","volume":"181","author":"Edwards","year":"2020","journal-title":"Cell"},{"key":"B40","doi-asserted-by":"publisher","first-page":"D427","DOI":"10.1093\/nar\/gky995","article-title":"The Pfam protein families database in 2019","volume":"47","author":"El-Gebali","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"B41","doi-asserted-by":"publisher","first-page":"e1001242","DOI":"10.1371\/journal.pbio.1001242","article-title":"Substrate specificity within a family of outer membrane carboxylate channels","volume":"10","author":"Eren","year":"2012","journal-title":"PLoS Biol."},{"key":"B42","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1016\/0378-1119(95)00049-C","article-title":"The sequencing of the 80-kDa D 15 protective surface antigen of Haemophilus influenzae","volume":"156","author":"Flack","year":"1995","journal-title":"Gene"},{"key":"B43","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1038\/nsb0198-37","article-title":"Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose","volume":"5","author":"Forst","year":"1998","journal-title":"Nat. Struct. Biol."},{"key":"B44","doi-asserted-by":"publisher","first-page":"1965","DOI":"10.1093\/bioinformatics\/btq308","article-title":"A highly accurate statistical approach for the prediction of transmembrane \u03b2-barrels","volume":"26","author":"Freeman","year":"2010","journal-title":"Bioinformatics"},{"key":"B45","doi-asserted-by":"publisher","first-page":"2425","DOI":"10.1093\/bioinformatics\/bts478","article-title":"TMBB-DB: a transmembrane \u03b2-barrel proteome database","volume":"28","author":"Freeman","year":"2012","journal-title":"Bioinformatics"},{"key":"B46","doi-asserted-by":"publisher","first-page":"843","DOI":"10.2174\/138920312804871120","article-title":"Microbe-host interactions: structure and role of gram-negative bacterial porins","volume":"13","author":"Galdiero","year":"2013","journal-title":"Curr. Protein Pept. Sci."},{"key":"B47","doi-asserted-by":"publisher","first-page":"104419","DOI":"10.1016\/j.micpath.2020.104419","article-title":"Evaluation of the \u03b2-barrel outer membrane protein VP1243 as a candidate antigen for a cross-protective vaccine against Vibrio infections","volume":"147","author":"Gao","year":"2020","journal-title":"Microb. Pathog."},{"key":"B48","doi-asserted-by":"publisher","first-page":"407","DOI":"10.1016\/j.resmic.2006.02.001","article-title":"Adhesion mediated by autotransporters of Gram-negative bacteria: structural and functional features","volume":"157","author":"Girard","year":"2006","journal-title":"Res. Microbiol."},{"key":"B49","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1186\/s12870-015-0445-1","article-title":"Oep23 forms an ion channel in the chloroplast outer envelope","volume":"15","author":"Goetze","year":"2015","journal-title":"BMC Plant Biol."},{"key":"B50","doi-asserted-by":"publisher","first-page":"17989","DOI":"10.1074\/jbc.M600700200","article-title":"OEP37 is a new member of the chloroplast outer membrane ion channels","volume":"281","author":"Goetze","year":"2006","journal-title":"J. Biol. Chem."},{"key":"B51","doi-asserted-by":"publisher","first-page":"1476","DOI":"10.1126\/science.283.5407.1476","article-title":"Mitochondrial evolution","volume":"283","author":"Gray","year":"1999","journal-title":"Science"},{"key":"B52","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1128\/9781555819286.ch8","article-title":"Bacterial secretion systems: an overview","volume":"4","author":"Green","year":"2016","journal-title":"Virulence Mech. Bact. Pathog. Fifth Ed."},{"key":"B53","doi-asserted-by":"publisher","first-page":"13308","DOI":"10.1038\/ncomms13308","article-title":"Structure of the bacterial plant-ferredoxin receptor FusA","volume":"31","author":"Grinter","year":"2016","journal-title":"Nat. Commun."},{"key":"B54","doi-asserted-by":"publisher","first-page":"1588","DOI":"10.1126\/science.3629258","article-title":"Biomaterial-centered infection: microbial adhesion versus tissue integration","volume":"237","author":"Gristina","year":"1987","journal-title":"Sci. Sciencemag Org."},{"key":"B55","doi-asserted-by":"publisher","first-page":"1027","DOI":"10.1111\/j.1365-2958.2003.03903.x","article-title":"Structure of the OmpA-like domain of RmpM from Neisseria meningitidis","volume":"51","author":"Grizot","year":"2004","journal-title":"Mol. Microbiol."},{"key":"B56","doi-asserted-by":"publisher","first-page":"D314","DOI":"10.1093\/nar\/gkl805","article-title":"TMBETA-GENOME: database for annotated beta-barrel membrane proteins in genomic sequences","volume":"35","author":"Gromiha","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"B57","doi-asserted-by":"publisher","first-page":"444","DOI":"10.1002\/2211-5463.12791","article-title":"Toc75-V\/OEP80 is processed during translocation into chloroplasts and the membrane embedded form exposes its POTRA domain to the intermembrane space","volume":"10","author":"Gross","year":"2020","journal-title":"FEBS Open Bio."},{"key":"B58","doi-asserted-by":"publisher","first-page":"496","DOI":"10.1016\/j.str.2015.01.001","article-title":"Lipopolysaccharide is inserted into the outer membrane through an intramembrane hole, a lumen gate, and the lateral opening of LptD","volume":"23","author":"Gu","year":"2015","journal-title":"Structure"},{"key":"B59","doi-asserted-by":"publisher","first-page":"1879","DOI":"10.1128\/JB.01796-07","article-title":"CmeR functions as a pleiotropic regulator and is required for optimal colonization of Campylobacter jejuni in vivo","volume":"190","author":"Guo","year":"2008","journal-title":"J. Bacteriol."},{"key":"B60","doi-asserted-by":"publisher","first-page":"17848","DOI":"10.1074\/jbc.M115.712398","article-title":"OEP40, a regulated glucose-permeable \u03b2-barrel solute channel in the chloroplast outer envelope membrane","volume":"291","author":"Harsman","year":"2016","journal-title":"J. Biol. Chem."},{"key":"B61","doi-asserted-by":"publisher","first-page":"12020","DOI":"10.1074\/jbc.M513586200","article-title":"Molecular properties of Oep21, an ATP-regulated anion-selective solute channel from the outer chloroplast membrane","volume":"281","author":"Hemmler","year":"2006","journal-title":"J. Biol. Chem."},{"key":"B62","doi-asserted-by":"publisher","first-page":"505","DOI":"10.1046\/j.1365-2958.1997.5921965.x","article-title":"Structural determinants of processing and secretion of the Haemophilus influenzae Hap protein","volume":"26","author":"Hendrixson","year":"1997","journal-title":"Mol. Microbiol."},{"key":"B63","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1046\/j.1365-2958.2002.02880.x","article-title":"Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA","volume":"44","author":"Higgs","year":"2002","journal-title":"Mol. Microbiol."},{"key":"B64","doi-asserted-by":"publisher","first-page":"516","DOI":"10.1038\/26780","article-title":"Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins","volume":"395","author":"Hill","year":"1998","journal-title":"Nature"},{"key":"B65","doi-asserted-by":"publisher","first-page":"899","DOI":"10.1016\/S0006-3495(02)75216-8","article-title":"The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides","volume":"83","author":"Hinnah","year":"2002","journal-title":"Biophys. J."},{"key":"B66","doi-asserted-by":"publisher","first-page":"eaah6834","DOI":"10.1126\/science.aah6834","article-title":"Membrane protein insertion through a mitochondrial \u03b2-barrel gate","volume":"359","author":"H\u00f6hr","year":"2018","journal-title":"Science"},{"key":"B67","doi-asserted-by":"publisher","first-page":"1005","DOI":"10.1002\/prot.24803","article-title":"Key challenges for the creation and maintenance of specialist protein resources","volume":"83","author":"Holliday","year":"2015","journal-title":"Proteins"},{"key":"B68","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1128\/MMBR.62.1.181-203.1998","article-title":"Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli","volume":"62","author":"H\u00f6ltje","year":"1998","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"B69","doi-asserted-by":"publisher","first-page":"12062","DOI":"10.1038\/ncomms12062","article-title":"Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process","volume":"13","author":"Iacovache","year":"2016","journal-title":"Nat. Commun."},{"key":"B70","doi-asserted-by":"publisher","first-page":"406","DOI":"10.1093\/nar\/gkg020","article-title":"TMPDB: a database of experimentally-characterized transmembrane topologies","volume":"31","author":"Ikeda","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"B71","doi-asserted-by":"publisher","first-page":"2126","DOI":"10.1074\/jbc.M114.584524","article-title":"Crystal structure of BamB bound to a periplasmic domain fragment of BamA, the central component of the \u03b2-barrel assembly machine","volume":"290","author":"Jansen","year":"2015","journal-title":"J. Biol. Chem."},{"key":"B72","first-page":"549","article-title":"Consensus based validation of membrane porins","volume":"4","author":"Katta","year":"2004","journal-title":"In Silico Biol."},{"key":"B73","doi-asserted-by":"publisher","first-page":"1821","DOI":"10.1128\/JCM.44.5.1821-1827.2006","article-title":"Development and evaluation of a rapid, simple, and sensitive immunochromatographic assay to detect thermostable direct hemolysin produced by Vibrio parahaemolyticus in enrichment cultures of stool specimens","volume":"44","author":"Kawatsu","year":"2006","journal-title":"J. Clin. Microbiol."},{"key":"B74","doi-asserted-by":"publisher","first-page":"845","DOI":"10.1038\/nprot.2015.053","article-title":"The Phyre2 web portal for protein modeling, prediction and analysis","volume":"10","author":"Kelley","year":"2015","journal-title":"Nat. Protoc."},{"key":"B75","doi-asserted-by":"publisher","first-page":"961","DOI":"10.1126\/science.1143993","article-title":"Structure and function of an essential component of the outer membrane protein assembly machine","volume":"317","author":"Kim","year":"2007","journal-title":"Science"},{"key":"B76","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1146\/annurev.arplant.043008.092119","article-title":"DNA transfer from organelles to the nucleus: the idiosyncratic genetics of endosymbiosis","volume":"60","author":"Kleine","year":"2009","journal-title":"Annu. Rev. Plant Biol."},{"key":"B77","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1016\/j.ijmm.2005.10.002","article-title":"Self-associating autotransporters, SAATs: functional and structural similarities","volume":"296","author":"Klemm","year":"2006","journal-title":"Int. J. Med. Microbiol."},{"key":"B78","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1046\/j.1365-2958.2000.01983.x","article-title":"Structure and function of bacterial outer membrane proteins: barrels in a nutshell","volume":"37","author":"Koebnik","year":"2000","journal-title":"Mol. Microbiol."},{"key":"B79","doi-asserted-by":"publisher","first-page":"e00371-17","DOI":"10.1128\/JB.00371-17","article-title":"Outer membrane permeability of cyanobacterium Synechocystis sp. strain PCC 6803: studies of passive diffusion of small organic nutrients reveal the absence of classical porins and intrinsically low permeability","volume":"199","author":"Kowata","year":"2017","journal-title":"J. Bacteriol."},{"key":"B80","doi-asserted-by":"publisher","first-page":"D524","DOI":"10.1093\/nar\/gks1169","article-title":"PDBTM: Protein data bank of transmembrane proteins after 8 years","volume":"41","author":"Kozma","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"B81","doi-asserted-by":"publisher","first-page":"215","DOI":"10.3389\/fcimb.2017.00215","article-title":"The Type IX Secretion System (T9SS): highlights and recent insights into its structure and function","volume":"7","author":"Lasica","year":"2017","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"B82","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1038\/s41586-018-0693-y","article-title":"Type 9 secretion system structures reveal a new protein transport mechanism","volume":"564","author":"Lauber","year":"2018","journal-title":"Nature"},{"key":"B83","doi-asserted-by":"publisher","first-page":"W580","DOI":"10.1093\/nar\/gkv279","article-title":"The EMBL-EBI bioinformatics web and programmatic tools framework","volume":"43","author":"Li","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"B84","doi-asserted-by":"publisher","first-page":"75","DOI":"10.3892\/ijmm.2012.967","article-title":"Molecular characterization of three major outer membrane proteins, TSA56, TSA47 and TSA22, in Orientia tsutsugamushi","volume":"30","author":"Lin","year":"2012","journal-title":"Int. J. Mol. Med."},{"key":"B85","doi-asserted-by":"publisher","first-page":"2319","DOI":"10.1021\/bi300066w","article-title":"OccK channels from Pseudomonas aeruginosa exhibit diverse single-channel electrical signatures but conserved anion selectivity","volume":"51","author":"Liu","year":"2012","journal-title":"Biochemistry"},{"key":"B86","doi-asserted-by":"publisher","first-page":"D370","DOI":"10.1093\/nar\/gkr703","article-title":"OPM database and PPM web server: resources for positioning of proteins in membranes","volume":"40","author":"Lomize","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"B87","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1007\/s10969-015-9194-5","article-title":"Annotation of proteins of unknown function: initial enzyme results","volume":"16","author":"McKay","year":"2015","journal-title":"J. Struct. Funct. Genomics"},{"key":"B88","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1016\/j.devcel.2004.06.003","article-title":"The mitochondrial morphology protein Mdm10 functions in assembly of the preprotein translocase of the outer membrane","volume":"7","author":"Meisinger","year":"2004","journal-title":"Dev. Cell"},{"key":"B89","doi-asserted-by":"publisher","first-page":"3864","DOI":"10.1038\/emboj.2011.279","article-title":"Crystal structure of the Haemophilus influenzae Hap adhesin reveals an intercellular oligomerization mechanism for bacterial aggregation","volume":"30","author":"Meng","year":"2011","journal-title":"EMBO J."},{"key":"B90","doi-asserted-by":"publisher","first-page":"5316","DOI":"10.1038\/s41467-018-07653-5","article-title":"CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers","volume":"9","author":"Menny","year":"2018","journal-title":"Nat. Commun."},{"key":"B91","doi-asserted-by":"publisher","first-page":"85","DOI":"10.1038\/nsmb1189","article-title":"An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane","volume":"14","author":"Moraes","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"B92","doi-asserted-by":"publisher","first-page":"482","DOI":"10.1016\/j.semcdb.2011.04.002","article-title":"Misfolded protein aggregates: mechanisms, structures and potential for disease transmission","volume":"22","author":"Moreno-Gonzalez","year":"2011","journal-title":"Semin. Cell Dev. Biol."},{"key":"B93","doi-asserted-by":"publisher","first-page":"1735","DOI":"10.1016\/j.bbamem.2007.07.015","article-title":"Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane-Distinct translocases and mechanisms","volume":"1778","author":"Natale","year":"2008","journal-title":"Biochim. Biophys. Acta - Biomembr."},{"key":"B94","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1016\/S1369-5274(99)80011-3","article-title":"Host cell interactions and signalling with Neisseria gonorrhoeae","volume":"2","author":"Naumann","year":"1999","journal-title":"Curr. Opin. Microbiol."},{"key":"B95","doi-asserted-by":"publisher","first-page":"D390","DOI":"10.1093\/nar\/gky1047","article-title":"The MemProtMD database: a resource for membrane-embedded protein structures and their lipid interactions","volume":"47","author":"Newport","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"B96","doi-asserted-by":"publisher","first-page":"328","DOI":"10.1099\/mic.0.024323-0","article-title":"Verification of a topology model of PorT as an integral outer-membrane protein in Porphyromonas gingivalis","volume":"155","author":"Nguyen","year":"2009","journal-title":"Microbiology"},{"key":"B97","doi-asserted-by":"publisher","first-page":"593","DOI":"10.1128\/MMBR.67.4.593-656.2003","article-title":"Molecular basis of bacterial outer membrane permeability revisited","volume":"67","author":"Nikaido","year":"2003","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"B98","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1016\/j.sbi.2015.02.012","article-title":"The \u03b2-barrel membrane protein insertase machinery from Gram-negative bacteria","volume":"31","author":"Noinaj","year":"2015","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B99","doi-asserted-by":"publisher","first-page":"422","DOI":"10.1016\/j.jmb.2007.07.003","article-title":"Bacterial sec-translocase unfolds and translocates a class of folded protein domains","volume":"372","author":"Nouwen","year":"2007","journal-title":"J. Mol. Biol."},{"key":"B100","doi-asserted-by":"publisher","first-page":"e0004988","DOI":"10.1371\/journal.pntd.0004988","article-title":"Characterizing the syphilis-causing Treponema pallidum ssp. pallidum proteome using complementary mass spectrometry","volume":"10","author":"Osbak","year":"2016","journal-title":"PLoS Negl. Trop. Dis."},{"key":"B101","doi-asserted-by":"publisher","first-page":"893","DOI":"10.1038\/nrmicro1994","article-title":"The porin and the permeating antibiotic: a selective diffusion barrier in Gram-negative bacteria","volume":"6","author":"Pag\u00e8s","year":"2008","journal-title":"Nat. Rev. Microbiol."},{"key":"B102","doi-asserted-by":"publisher","first-page":"D663","DOI":"10.1093\/nar\/gkv1271","article-title":"PSORTdb: expanding the bacteria and archaea protein subcellular localization database to better reflect diversity in cell envelope structures","volume":"44","author":"Peabody","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"B103","doi-asserted-by":"publisher","first-page":"785","DOI":"10.1038\/nmeth.1701","article-title":"SignalP 4.0: discriminating signal peptides from transmembrane regions","volume":"8","author":"Petersen","year":"2011","journal-title":"Nat. Methods"},{"key":"B104","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1016\/j.cell.2006.02.012","article-title":"Bacterial adhesion and entry into host cells","volume":"124","author":"Pizarro-Cerd\u00e1","year":"2006","journal-title":"Cell"},{"key":"B105","doi-asserted-by":"publisher","first-page":"268","DOI":"10.1084\/jem.156.1.268","article-title":"Molecular organization of C9 within the membrane attack complex of complement. induction of circular C9 polymerization by the C5b-8 assembly","volume":"156","author":"Podack","year":"1982","journal-title":"J. Exp. Med."},{"key":"B106","doi-asserted-by":"publisher","first-page":"11598","DOI":"10.1038\/ncomms11598","article-title":"Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly","volume":"7","author":"Podobnik","year":"2016","journal-title":"Nat. Commun."},{"key":"B107","doi-asserted-by":"publisher","first-page":"1207","DOI":"10.1105\/tpc.10.7.1207","article-title":"A high-conductance solute channel in the chloroplastic outer envelope from Pea","volume":"10","author":"Pohlmeyer","year":"1998","journal-title":"Plant Cell"},{"key":"B108","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1007\/s00018-005-5350-6","article-title":"The membrane protein data bank","volume":"63","author":"Raman","year":"2006","journal-title":"Cell. Mol. Life Sci."},{"key":"B109","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1038\/nature06384","article-title":"Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes","volume":"450","author":"Rapoport","year":"2007","journal-title":"Nature"},{"key":"B110","doi-asserted-by":"publisher","first-page":"W446","DOI":"10.1093\/nar\/gkp325","article-title":"HHomp\u2013prediction and classification of outer membrane proteins","volume":"37","author":"Remmert","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"B111","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1002\/1439-7633(20020503)3:5","article-title":"OmpA membrane domain as a tight-binding anchor for lipid bilayers","volume":"3","author":"Ringler","year":"2002","journal-title":"ChemBioChem"},{"key":"B112","doi-asserted-by":"publisher","first-page":"1548","DOI":"10.1126\/science.1144706","article-title":"A common fold mediates vertebrate defense and bacterial attack","volume":"317","author":"Rosado","year":"2007","journal-title":"Science"},{"key":"B113","doi-asserted-by":"publisher","first-page":"1209","DOI":"10.1021\/acs.jproteome.9b00740","article-title":"Landscape of eukaryotic transmembrane beta barrel proteins","volume":"19","author":"Roumia","year":"2020","journal-title":"J. Proteome Res."},{"key":"B114","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1038\/s41467-017-00361-6","article-title":"A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis","volume":"8","author":"Rouse","year":"2017","journal-title":"Nat. Commun."},{"key":"B115","doi-asserted-by":"publisher","first-page":"3161","DOI":"10.1128\/IAI.64.8.3161-3167.1996","article-title":"Cloning, sequencing, expression, and protective capacity of the oma87 gene encoding the Pasteurella multocida 87-kilodalton outer membrane antigen","volume":"64","author":"Ruffolo","year":"1996","journal-title":"Infect. Immun."},{"key":"B116","doi-asserted-by":"publisher","first-page":"7071","DOI":"10.1073\/pnas.0509392103","article-title":"Crystal structure and catalytic mechanism of the LPS 3-O-deacylase PagL from Pseudomonas aeruginosa","volume":"103","author":"Rutten","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B117","doi-asserted-by":"publisher","first-page":"D372","DOI":"10.1093\/nar\/gkv1103","article-title":"The Transporter Classification Database (TCDB): recent advances","volume":"44","author":"Saier","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"B118","doi-asserted-by":"publisher","first-page":"D5","DOI":"10.1093\/nar\/gkp382","article-title":"Database resources of the national center for biotechnology information","volume":"37","author":"Sayers","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"B119","doi-asserted-by":"publisher","first-page":"512","DOI":"10.1126\/science.7824948","article-title":"Structural basis for sugar translocation through maltoporin channels at 3.1 \u00c5 resolution","volume":"267","author":"Schirmer","year":"1995","journal-title":"Science"},{"key":"B120","doi-asserted-by":"publisher","first-page":"308","DOI":"10.1016\/S0005-2736(02)00577-1","article-title":"The structure of bacterial outer membrane proteins","volume":"1565","author":"Schulz","year":"2002","journal-title":"Biochim. Biophys. Acta"},{"key":"B121","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.celrep.2016.03.002","article-title":"Heterogeneous MAC Initiator and pore structures in a lipid bilayer by phase-plate cryo-electron tomography","volume":"15","author":"Sharp","year":"2016","journal-title":"Cell Rep."},{"key":"B122","doi-asserted-by":"publisher","first-page":"293","DOI":"10.1016\/S0092-8674(00)81660-8","article-title":"The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins","volume":"99","author":"Shatursky","year":"1999","journal-title":"Cell"},{"key":"B123","doi-asserted-by":"publisher","first-page":"14563","DOI":"10.1021\/bi981452f","article-title":"Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy","volume":"37","author":"Shepard","year":"1998","journal-title":"Biochemistry"},{"key":"B124","doi-asserted-by":"publisher","first-page":"1008","DOI":"10.1016\/j.bpj.2016.07.043","article-title":"The screw-like movement of a gliding bacterium is powered by spiral motion of cell-surface adhesins","volume":"111","author":"Shrivastava","year":"2016","journal-title":"Biophys. J."},{"key":"B125","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1038\/nrm1333","article-title":"Protein import into chloroplasts","volume":"9","author":"Soll","year":"2004","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B126","doi-asserted-by":"publisher","first-page":"1059","DOI":"10.1128\/JB.181.4.1059-1071.1999","article-title":"MINIREVIEW bacterial adhesins: common themes and variations in architecture and assembly","volume":"181","author":"Soto","year":"1999","journal-title":"J. Bacteriol."},{"key":"B127","doi-asserted-by":"publisher","first-page":"4318","DOI":"10.1016\/S0021-9258(18)32625-5","article-title":"Evidence of direct insertion of terminal complement proteins into cell membrane bilayers during cytolysis. labeling by a photosensitive membrane probe reveals a major role for the eighth and ninth components","volume":"258","author":"Steckel","year":"1983","journal-title":"J. Biol. Chem."},{"key":"B128","doi-asserted-by":"publisher","first-page":"881","DOI":"10.1083\/jcb.200706043","article-title":"Alternative function for the mitochondrial SAM complex in biogenesis of \u03b1-helical TOM proteins","volume":"179","author":"Stojanovski","year":"2007","journal-title":"J. Cell Biol."},{"key":"B129","doi-asserted-by":"publisher","first-page":"729","DOI":"10.1006\/jmbi.1997.1348","article-title":"Common core structure of amyloid fibrils by synchrotron X-ray diffraction","volume":"273","author":"Sunde","year":"1997","journal-title":"J. Mol. Biol."},{"key":"B130","doi-asserted-by":"publisher","first-page":"464","DOI":"10.1016\/j.tim.2010.06.005","article-title":"A phylum level perspective on bacterial cell envelope architecture","volume":"18","author":"Sutcliffe","year":"2010","journal-title":"Trends Microbiol."},{"key":"B131","doi-asserted-by":"publisher","first-page":"D506","DOI":"10.1093\/nar\/gky1049","article-title":"UniProt: a worldwide hub of protein knowledge","volume":"47","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"B132","doi-asserted-by":"publisher","first-page":"e36523","DOI":"10.1371\/journal.pone.0036523","article-title":"DipA, a pore-forming protein in the outer membrane of Lyme disease spirochetes exhibits specificity for the permeation of dicarboxylates","volume":"7","author":"Thein","year":"2012","journal-title":"PLoS ONE"},{"key":"B133","doi-asserted-by":"publisher","first-page":"7035","DOI":"10.1128\/JB.00818-08","article-title":"Oms38 is the first identified pore-forming protein in the outer membrane of relapsing fever spirochetes","volume":"190","author":"Thein","year":"2008","journal-title":"J. Bacteriol."},{"key":"B134","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1016\/j.mib.2021.01.009","article-title":"The assembly of \u03b2-barrel outer membrane proteins","volume":"60","author":"Tomasek","year":"2021","journal-title":"Curr. Opin. Microbiol."},{"key":"B135","doi-asserted-by":"publisher","first-page":"e0221588","DOI":"10.1371\/journal.pone.0221588","article-title":"Analysis of the 56-kDa type specific antigen gene of Orientia tsutsugamushi from northern Vietnam","volume":"14","author":"Trung","year":"2019","journal-title":"PLoS ONE"},{"key":"B136","doi-asserted-by":"publisher","first-page":"831","DOI":"10.1038\/322831a0","article-title":"Structural\/functional similarity between proteins involved in complement- and cytotoxic T-lymphocyte-mediated cytolysis","volume":"322","author":"Tschopp","year":"1986","journal-title":"Nature"},{"key":"B137","doi-asserted-by":"publisher","first-page":"D324","DOI":"10.1093\/nar\/gkq863","article-title":"OMPdb: a database of {beta}-barrel outer membrane proteins from Gram-negative bacteria","volume":"39","author":"Tsirigos","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"B138","doi-asserted-by":"publisher","first-page":"i665","DOI":"10.1093\/bioinformatics\/btw444","article-title":"PRED-TMBB2: improved topology prediction and detection of beta-barrel outer membrane proteins","volume":"32","author":"Tsirigos","year":"2016","journal-title":"Bioinformatics"},{"key":"B139","doi-asserted-by":"publisher","first-page":"D234","DOI":"10.1093\/nar\/gkm751","article-title":"TOPDB: topology data bank of transmembrane proteins","volume":"36","author":"Tusn\u00e1dy","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"B140","doi-asserted-by":"publisher","first-page":"41044","DOI":"10.1074\/jbc.M112.408518","article-title":"Structural basis for outer membrane sugar uptake in pseudomonads","volume":"287","author":"Van Den Berg","year":"2012","journal-title":"J. Biol. Chem."},{"key":"B141","doi-asserted-by":"publisher","first-page":"11927","DOI":"10.1038\/srep11927","article-title":"Crystal structure of a COG4313 outer membrane channel","volume":"5","author":"van den Berg","year":"2015","journal-title":"Sci. Rep."},{"key":"B142","doi-asserted-by":"publisher","first-page":"1506","DOI":"10.1126\/science.1097524","article-title":"Crystal structure of the long-chain fatty acid transporter FadL","volume":"304","author":"van den Berg","year":"2004","journal-title":"Science"},{"key":"B143","doi-asserted-by":"publisher","first-page":"6741","DOI":"10.1128\/IAI.70.12.6741-6750.2002","article-title":"Cloning and porin activity of the major outer membrane protein P1 from Coxiella burnetii","volume":"70","author":"Varghees","year":"2002","journal-title":"Infect. Immun."},{"key":"B144","doi-asserted-by":"publisher","first-page":"7074","DOI":"10.1128\/JB.00737-09","article-title":"The beta-barrel outer membrane protein assembly complex of Neisseria Meningitidis","volume":"191","author":"Volokhina","year":"2009","journal-title":"J. Bacteriol."},{"key":"B145","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1017\/S0033583500003541","article-title":"Recent advances in the understanding of membrane protein assembly and structure","volume":"32","author":"von Heijne","year":"1999","journal-title":"Q. Rev. Biophys."},{"key":"B146","doi-asserted-by":"publisher","first-page":"19109","DOI":"10.1073\/pnas.0505033102","article-title":"Microarray-based detection of genetic heterogeneity, antimicrobial resistance, and the viable but nonculturable state in human pathogenic Vibrio spp","volume":"102","author":"Vora","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B147","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1126\/science.1078973","article-title":"Role of a highly conserved bacterial protein in outer membrane protein assembly","volume":"299","author":"Voulhoux","year":"2003","journal-title":"Science"},{"key":"B148","doi-asserted-by":"publisher","first-page":"6441","DOI":"10.1128\/JB.179.20.6441-6447.1997","article-title":"Identification, isolation, and characterization of the 42-kilodalton major outer membrane protein (MompA) from Treponema pectinovorum ATCC 33768","volume":"179","author":"Walker","year":"1997","journal-title":"J. Bacteriol."},{"key":"B149","doi-asserted-by":"publisher","first-page":"01","DOI":"10.1046\/j.1365-2958.1999.01339.x","article-title":"Type IV pili and cell motility","volume":"32","author":"Wall","year":"1999","journal-title":"Mol. Microbiol."},{"key":"B150","doi-asserted-by":"publisher","first-page":"10046","DOI":"10.1074\/jbc.M115.711762","article-title":"Structural basis for translocation of a biofilm-supporting exopolysaccharide across the bacterial outer membrane","volume":"291","author":"Wang","year":"2016","journal-title":"J. Biol. Chem."},{"key":"B151","doi-asserted-by":"publisher","first-page":"56","DOI":"10.1006\/jmbi.1997.1224","article-title":"Channel specificity: Structural basis for sugar discrimination and differential flux rates in maltoporin","volume":"272","author":"Wang","year":"1997","journal-title":"J. Mol. Biol."},{"key":"B152","doi-asserted-by":"publisher","first-page":"614","DOI":"10.1111\/j.1365-313X.2012.04900.x","article-title":"TGD4 involved in endoplasmic reticulum-to-chloroplast lipid trafficking is a phosphatidic acid binding protein","volume":"70","author":"Wang","year":"2012","journal-title":"Plant J."},{"key":"B153","doi-asserted-by":"publisher","first-page":"344","DOI":"10.1038\/nature08142","article-title":"Biophysical dissection of membrane proteins","volume":"459","author":"White","year":"2009","journal-title":"Nature"},{"key":"B154","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1146\/annurev-biochem-060713-035600","article-title":"Biosynthesis and export of bacterial lipopolysaccharides","volume":"83","author":"Whitfield","year":"2014","journal-title":"Annu. Rev. Biochem."},{"key":"B155","doi-asserted-by":"publisher","first-page":"718","DOI":"10.1016\/j.jmb.2009.09.054","article-title":"NanC crystal structure, a model for outer-membrane channels of the acidic sugar-specific KdgM porin family","volume":"394","author":"Wirth","year":"2009","journal-title":"J. Mol. Biol."},{"key":"B156","doi-asserted-by":"publisher","first-page":"643","DOI":"10.1002\/prot.21018","article-title":"Prediction of protein subcellular localization","volume":"64","author":"Yu","year":"2006","journal-title":"Proteins"},{"key":"B157","doi-asserted-by":"publisher","first-page":"1608","DOI":"10.1093\/bioinformatics\/btq249","article-title":"PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes","volume":"26","author":"Yu","year":"2010","journal-title":"Bioinformatics"},{"key":"B158","doi-asserted-by":"publisher","first-page":"779","DOI":"10.1016\/j.mib.2013.09.007","article-title":"On the essentiality of lipopolysaccharide to Gram-negative bacteria","volume":"16","author":"Zhang","year":"2013","journal-title":"Curr. Opin. Microbiol."},{"key":"B159","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1007\/s00253-013-5355-2","article-title":"Deletion of the Cytophaga hutchinsonii type IX secretion system gene sprP results in defects in gliding motility and cellulose utilization","volume":"98","author":"Zhu","year":"2014","journal-title":"Appl. Microbiol. Biotechnol."}],"container-title":["Frontiers in Bioinformatics"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fbinf.2021.646581\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,4,9]],"date-time":"2021-04-09T06:54:59Z","timestamp":1617951299000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fbinf.2021.646581\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,4,9]]},"references-count":159,"alternative-id":["10.3389\/fbinf.2021.646581"],"URL":"https:\/\/doi.org\/10.3389\/fbinf.2021.646581","relation":{},"ISSN":["2673-7647"],"issn-type":[{"type":"electronic","value":"2673-7647"}],"subject":[],"published":{"date-parts":[[2021,4,9]]},"article-number":"646581"}}