{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T23:47:56Z","timestamp":1788047276516,"version":"build-2784847793"},"reference-count":46,"publisher":"American Society for Microbiology","issue":"4","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Bacteriology"],"published-print":{"date-parts":[[2013,2,15]]},"DOI":"10.1128\/jb.01355-12","type":"journal-article","created":{"date-parts":[[2012,12,8]],"date-time":"2012-12-08T08:19:12Z","timestamp":1354954752000},"page":"788-797","source":"Crossref","is-referenced-by-count":19,"title":["System Specificity of the TpsB Transporters of Coexpressed Two-Partner Secretion Systems of Neisseria meningitidis"],"prefix":"10.1128","volume":"195","author":[{"given":"S.","family":"ur Rahman","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P.","family":"van Ulsen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","published-online":{"date-parts":[[2012,12,7]]},"reference":[{"key":"key20180919081205_B1","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1046\/j.1365-2958.2001.02278.x","article-title":"Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins","volume":"40","author":"Jacob-Dubuisson","year":"2001","journal-title":"Mol. Microbiol."},{"key":"key20180919081205_B2","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.bbamcr.2004.03.008","article-title":"Protein secretion through autotransporter and two-partner pathways","volume":"1694","author":"Jacob-Dubuisson","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"key20180919081205_B3","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1146\/annurev.genet.42.110807.091449","article-title":"Bacterial contact-dependent delivery systems","volume":"44","author":"Hayes","year":"2010","journal-title":"Annu. Rev. Genet."},{"key":"key20180919081205_B4","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1016\/S1286-4579(00)00356-7","article-title":"Epidemiology and pathogenesis of Neisseria meningitidis","volume":"2","author":"Tzeng","year":"2000","journal-title":"Microbes Infect."},{"key":"key20180919081205_B5","doi-asserted-by":"crossref","first-page":"4649","DOI":"10.1128\/IAI.00393-08","article-title":"Two-partner secretion systems of Neisseria meningitidis associated with invasive clonal complexes","volume":"76","author":"van Ulsen","year":"2008","journal-title":"Infect. Immun."},{"key":"key20180919081205_B6","doi-asserted-by":"crossref","first-page":"7968","DOI":"10.1128\/JB.00851-07","article-title":"A functional two-partner secretion system contributes to adhesion of Neisseria meningitidis to epithelial cells","volume":"189","author":"Schmitt","year":"2007","journal-title":"J. Bacteriol."},{"key":"key20180919081205_B7","doi-asserted-by":"crossref","first-page":"2461","DOI":"10.1111\/j.1462-5822.2008.01222.x","article-title":"The HrpB-HrpA two-partner secretion system is essential for intracellular survival of Neisseria meningitidis","volume":"10","author":"Tala","year":"2008","journal-title":"Cell. Microbiol."},{"key":"key20180919081205_B8","doi-asserted-by":"crossref","first-page":"e1002217","DOI":"10.1371\/journal.pgen.1002217","article-title":"Identification of Functional Toxin\/Immunity Genes Linked to Contact-Dependent Growth Inhibition (CDI) and Rearrangement Hotspot (Rhs) Systems","volume":"7","author":"Poole","year":"2011","journal-title":"PLoS Genet."},{"key":"key20180919081205_B9","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1126\/science.287.5459.1809","article-title":"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58","volume":"287","author":"Tettelin","year":"2000","journal-title":"Science"},{"key":"key20180919081205_B10","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1111\/j.1574-6976.2006.00013.x","article-title":"Protein secretion and secreted proteins in pathogenic Neisseriaceae","volume":"30","author":"van Ulsen","year":"2006","journal-title":"FEMS Microbiol. Rev."},{"key":"key20180919081205_B11","doi-asserted-by":"crossref","first-page":"2371","DOI":"10.1128\/JB.01331-10","article-title":"Genome sequence of Neisseria meningitidis serogroup B strain H44\/76","volume":"193","author":"Piet","year":"2011","journal-title":"J. Bacteriol."},{"key":"key20180919081205_B12","doi-asserted-by":"crossref","first-page":"4494","DOI":"10.1073\/pnas.1019751108","article-title":"Neisseria meningitidis is structured in clades associated with restriction modification systems that modulate homologous recombination","volume":"108","author":"Budroni","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"key20180919081205_B13","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1128\/jb.178.4.1053-1060.1996","article-title":"Distinct roles of the N-terminal and C-terminal precursor domains in the biogenesis of the Bordetella pertussis filamentous hemagglutinin","volume":"178","author":"Renauld-Mong\u00e9nie","year":"1996","journal-title":"J. Bacteriol."},{"key":"key20180919081205_B14","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1128\/jb.179.3.775-783.1997","article-title":"Lack of functional complementation between Bordetella pertussis filamentous hemagglutinin and Proteus mirabilis HpmA hemolysin secretion machineries","volume":"179","author":"Jacob-Dubuisson","year":"1997","journal-title":"J. Bacteriol."},{"key":"key20180919081205_B15","doi-asserted-by":"crossref","first-page":"4658","DOI":"10.1128\/IAI.68.8.4658-4665.2000","article-title":"Characterization of adherence of non-typeable Haemophilus influenzae to human epithelial cells","volume":"68","author":"Van Schilfgaarde","year":"2000","journal-title":"Infect. Immun."},{"key":"key20180919081205_B16","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1016\/j.ijmm.2010.08.005","article-title":"Protein secretion systems in Pseudomonas aeruginosa: a wealth of pathogenic weapons","volume":"300","author":"Bleves","year":"2010","journal-title":"Int. J. Med. Microbiol."},{"key":"key20180919081205_B17","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/S0092-8674(00)80743-6","article-title":"A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein","volume":"97","author":"Spiess","year":"1999","journal-title":"Cell"},{"key":"key20180919081205_B18","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1046\/j.1365-2958.2003.03773.x","article-title":"A neisserial autotransporter NaIP modulating the processing of other autotransporters","volume":"50","author":"van Ulsen","year":"2003","journal-title":"Mol. Microbiol."},{"key":"key20180919081205_B19","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/0378-1119(95)00108-I","article-title":"Improved antibiotic-resistance gene cassettes and omega-elements for Escherichia-coli vector construction and in-vitro deletion insertion mutagenesis","volume":"160","author":"Alexeyev","year":"1995","journal-title":"Gene"},{"key":"key20180919081205_B20","doi-asserted-by":"crossref","first-page":"6194","DOI":"10.1073\/pnas.0400291101","article-title":"The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway","volume":"101","author":"Clantin","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"key20180919081205_B21","doi-asserted-by":"crossref","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":"key20180919081205_B22","doi-asserted-by":"crossref","first-page":"W13","DOI":"10.1093\/nar\/gkr245","article-title":"T-Coffee: a web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension","volume":"39","author":"Di Tommaso","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"key20180919081205_B23","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1038\/nprot.2009.2","article-title":"Protein structure prediction on the Web: a case study using the Phyre server","volume":"4","author":"Kelley","year":"2009","journal-title":"Nat. Protoc."},{"key":"key20180919081205_B24","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1038\/nprot.2010.5","article-title":"I-TASSER: a unified platform for automated protein structure and function prediction","volume":"5","author":"Roy","year":"2010","journal-title":"Nat. Protoc."},{"key":"key20180919081205_B25","doi-asserted-by":"crossref","first-page":"2302","DOI":"10.1093\/nar\/gki524","article-title":"TM-align: a protein structure alignment algorithm based on the TM-score","volume":"33","author":"Zhang","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"key20180919081205_B26","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1111\/j.1365-2958.1993.tb01252.x","article-title":"Amino-acid replacements in the Serratia-marcescens hemolysin ShlA define sites involved in activation and secretion","volume":"9","author":"Sch\u00f6nherr","year":"1993","journal-title":"Mol. Microbiol."},{"key":"key20180919081205_B27","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1046\/j.1365-2958.2000.01812.x","article-title":"Maturation and secretion of the non-typable Haemophilus influenzae HMW1 adhesin: roles of the N-terminal and C-terminal domains","volume":"36","author":"Grass","year":"2000","journal-title":"Mol. Microbiol."},{"key":"key20180919081205_B28","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1126\/science.1143860","article-title":"Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily","volume":"317","author":"Clantin","year":"2007","journal-title":"Science"},{"key":"key20180919081205_B29","doi-asserted-by":"crossref","first-page":"22297","DOI":"10.1074\/jbc.M109.014431","article-title":"Structural and functional studies of truncated hemolysin A from Proteus mirabilis","volume":"284","author":"Weaver","year":"2009","journal-title":"J. Biol. Chem."},{"key":"key20180919081205_B30","doi-asserted-by":"crossref","first-page":"5040","DOI":"10.1093\/emboj\/20.18.5040","article-title":"Subtilisin-like autotransporter serves as maturation protease in a bacterial secretion pathway","volume":"20","author":"Coutte","year":"2001","journal-title":"EMBO J."},{"key":"key20180919081205_B31","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1046\/j.1365-2958.2003.03450.x","article-title":"The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires HMW1C and phosphoglucomutase, an enzyme involved in lipooligosaccharide biosynthesis","volume":"48","author":"Grass","year":"2003","journal-title":"Mol. Microbiol."},{"key":"key20180919081205_B32","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1111\/j.1365-2958.2006.05392.x","article-title":"Topology and maturation of filamentous haemagglutinin suggest a new model for two-partner secretion","volume":"62","author":"Mazar","year":"2006","journal-title":"Mol. Microbiol."},{"key":"key20180919081205_B33","doi-asserted-by":"crossref","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":"key20180919081205_B34","doi-asserted-by":"crossref","first-page":"e1000572","DOI":"10.1371\/journal.ppat.1000572","article-title":"A novel extracytoplasmic function (ECF) sigma factor regulates virulence in Pseudomonas aeruginosa","volume":"5","author":"Llamas","year":"2009","journal-title":"PLoS Pathog."},{"key":"key20180919081205_B35","doi-asserted-by":"crossref","first-page":"1524","DOI":"10.1111\/j.1365-2958.2007.05605.x","article-title":"Limited tolerance towards folded elements during secretion of the autotransporter Hbp","volume":"63","author":"Jong","year":"2007","journal-title":"Mol. Microbiol."},{"key":"key20180919081205_B36","doi-asserted-by":"crossref","first-page":"38224","DOI":"10.1074\/jbc.M110.180505","article-title":"A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocation","volume":"285","author":"Soprova","year":"2010","journal-title":"J. Biol. Chem."},{"key":"key20180919081205_B37","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1111\/j.1365-2958.2009.06860.x","article-title":"Role of DegP for two-partner secretion in Bordetella","volume":"74","author":"Baud","year":"2009","journal-title":"Mol. Microbiol."},{"key":"key20180919081205_B38","doi-asserted-by":"crossref","first-page":"31076","DOI":"10.1074\/jbc.M705750200","article-title":"The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion","volume":"282","author":"Yeo","year":"2007","journal-title":"J. Biol. Chem."},{"key":"key20180919081205_B39","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1111\/j.1365-2958.2009.06993.x","article-title":"Sequential translocation of an Escherichia coli two-partner secretion pathway exoprotein across the inner and outer membranes","volume":"75","author":"Choi","year":"2010","journal-title":"Mol. Microbiol."},{"key":"key20180919081205_B40","doi-asserted-by":"crossref","first-page":"2765","DOI":"10.1128\/IAI.00079-07","article-title":"Moraxella catarrhalis strain O35E expresses two filamentous hemagglutinin-like proteins that mediate adherence to human epithelial cells","volume":"75","author":"Balder","year":"2007","journal-title":"Infect. Immun."},{"key":"key20180919081205_B41","doi-asserted-by":"crossref","first-page":"1874","DOI":"10.1128\/IAI.72.4.1874-1884.2004","article-title":"The LspB protein is involved in the secretion of the LspA1 and LspA2 proteins by Haemophilus ducreyi","volume":"72","author":"Ward","year":"2004","journal-title":"Infect. Immun."},{"key":"key20180919081205_B42","doi-asserted-by":"crossref","first-page":"2669","DOI":"10.1038\/emboj.2008.197","article-title":"The \u2018P-usher\u2019, a novel protein transporter involved in fimbrial assembly and TpsA secretion","volume":"27","author":"Ruer","year":"2008","journal-title":"EMBO J."},{"key":"key20180919081205_B43","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1515\/BC.2009.099","article-title":"First structural insights into the TpsB\/Omp85 superfamily","volume":"390","author":"Jacob-Dubuisson","year":"2009","journal-title":"Biol. Chem."},{"key":"key20180919081205_B44","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1111\/j.1365-2958.2011.07680.x","article-title":"Substrate recognition by the POTRA domains of TpsB transporter FhaC","volume":"81","author":"Delattre","year":"2011","journal-title":"Mol. Microbiol."},{"key":"key20180919081205_B45","doi-asserted-by":"crossref","DOI":"10.1111\/mmi.12036","article-title":"The prodomain of the Bordetella two-partner secretion pathway protein FhaB","author":"No\u00ebl","year":"2012","journal-title":"Mol. Microbiol."},{"key":"key20180919081205_B46","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1371\/journal.pgen.0030023","article-title":"Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18","volume":"3","author":"Bentley","year":"2007","journal-title":"PLoS Genet."}],"container-title":["Journal of Bacteriology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1128\/JB.01355-12","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T17:33:59Z","timestamp":1627580039000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/JB.01355-12"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,12,7]]},"references-count":46,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2013,1,25]]},"published-print":{"date-parts":[[2013,2,15]]}},"URL":"https:\/\/doi.org\/10.1128\/jb.01355-12","relation":{},"ISSN":["0021-9193"],"issn-type":[{"value":"0021-9193","type":"print"}],"subject":[],"published":{"date-parts":[[2012,12,7]]}}}