{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T13:31:34Z","timestamp":1790602294868,"version":"4.1.0"},"reference-count":48,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2014,3,15]],"date-time":"2014-03-15T00:00:00Z","timestamp":1394841600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2014,3,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    We recently showed that type II signal peptidase (SPaseII) encoded by\n                    <jats:italic>lspA<\/jats:italic>\n                    is the target of an antibiotic called TA (myxovirescin), which is made by\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Myxococcus xanthus<\/jats:named-content>\n                    . SPaseII cleaves the signal peptide during bacterial lipoprotein processing. Bacteria typically contain one\n                    <jats:italic>lspA<\/jats:italic>\n                    gene; however, strikingly, the\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">M. xanthus<\/jats:named-content>\n                    DK1622 genome contains four (\n                    <jats:italic>lspA1<\/jats:italic>\n                    to\n                    <jats:italic>lspA4<\/jats:italic>\n                    ). Since two of these genes,\n                    <jats:italic>lspA3<\/jats:italic>\n                    and\n                    <jats:italic>lspA4<\/jats:italic>\n                    , are located in the giant TA biosynthetic gene cluster, we hypothesized they may play a role in TA resistance. To investigate the functions of the four\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">M. xanthus<\/jats:named-content>\n                    <jats:italic>lspA<\/jats:italic>\n                    (\n                    <jats:italic>lspA<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>Mx<\/jats:italic>\n                    <\/jats:sup>\n                    ) genes, we conducted sequence comparisons and found that they contained nearly all the conserved residues characteristic of SPaseII family members. Genetic studies found that an\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>\n                    \u0394\n                    <jats:italic>lspA<\/jats:italic>\n                    mutation could be complemented by any of the\n                    <jats:italic>lspA<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>Mx<\/jats:italic>\n                    <\/jats:sup>\n                    genes in an\n                    <jats:italic>lpp<\/jats:italic>\n                    mutant background, but not in an\n                    <jats:italic>E. coli lpp<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>+<\/jats:italic>\n                    <\/jats:sup>\n                    background. Because Lpp is the most abundant\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n                    lipoprotein, these results suggest the\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">M. xanthus<\/jats:named-content>\n                    proteins do not function as efficiently as the host enzyme. In\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n                    , overexpression of each of the LspA\n                    <jats:sup>\n                      <jats:italic>Mx<\/jats:italic>\n                    <\/jats:sup>\n                    proteins conferred TA and globomycin resistance, although LspA3 conferred the highest degree of resistance. In\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">M. xanthus<\/jats:named-content>\n                    , each\n                    <jats:italic>lspA<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>Mx<\/jats:italic>\n                    <\/jats:sup>\n                    gene could be deleted and was therefore dispensable for growth. However,\n                    <jats:italic>lspA3<\/jats:italic>\n                    or\n                    <jats:italic>lspA4<\/jats:italic>\n                    deletion mutants each exhibited a tan phase variation bias, which likely accounts for their reduced-swarming and delayed-development phenotypes. In summary, we propose that all four LspA\n                    <jats:sup>\n                      <jats:italic>Mx<\/jats:italic>\n                    <\/jats:sup>\n                    proteins function as SPaseIIs and that LspA3 and LspA4 might also have roles in TA resistance and regulation, respectively.\n                  <\/jats:p>","DOI":"10.1128\/jb.01361-13","type":"journal-article","created":{"date-parts":[[2014,1,3]],"date-time":"2014-01-03T22:13:10Z","timestamp":1388787190000},"page":"1174-1183","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":32,"title":["Genetic Redundancy, Proximity, and Functionality of\n                    <i>lspA<\/i>\n                    , the Target of Antibiotic TA, in the Myxococcus xanthus Producer Strain"],"prefix":"10.1128","volume":"196","author":[{"given":"Yao","family":"Xiao","sequence":"first","affiliation":[{"name":"Department of Molecular Biology, University of Wyoming, Laramie, Wyoming, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Wall","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology, University of Wyoming, Laramie, Wyoming, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1039\/b901287g"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.06148-11"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.7164\/antibiotics.35.1454"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.4.5.507"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.7164\/antibiotics.37.13"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-894X(02)01024-7"},{"key":"e_1_3_3_8_2","doi-asserted-by":"crossref","first-page":"439","DOI":"10.7164\/antibiotics.41.439","article-title":"Novel macrocyclic antibiotics: megovalicins A, B, C, D, G and H. II. Isolation and chemical structures of megovalicins","volume":"41","author":"Takayama S","year":"1988","unstructured":"TakayamaSYamanakaSMiyashiroSYokokawaYShibaiH. 1988. Novel macrocyclic antibiotics: megovalicins A, B, C, D, G and H. II. Isolation and chemical structures of megovalicins. J. Antibiot. (Tokyo) 41:439\u2013445.","journal-title":"J. Antibiot. (Tokyo)"},{"key":"e_1_3_3_9_2","first-page":"1005","volume-title":"Escherichia coli and Salmonella","author":"Wu HC","year":"1996","unstructured":"WuHC. 1996. Biosynthesis of lipoproteins, p 1005\u20131014. In NeidhardtFCCurtissRIIIIngrahamJLLinECCLowKBMagasanikBReznikoffWSRileyMSchaechterMUmbargerHE (ed), Escherichia coli and Salmonella, 2nd ed, vol I. ASM Press, Washington, DC.","edition":"2"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF00763177"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro2814"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00203-005-0067-3"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1007\/s13238-012-2023-8"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tim.2008.10.001"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1999.01247.x"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1099\/mic.0.2006\/000216-0"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)44136-6"},{"key":"e_1_3_3_18_2","doi-asserted-by":"crossref","first-page":"17667","DOI":"10.1016\/S0021-9258(19)47423-1","article-title":"Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II)","volume":"266","author":"Munoa FJ","year":"1991","unstructured":"MunoaFJMillerKWBeersRGrahamMWuHC. 1991. Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II). J. Biol. Chem. 266:17667\u201317672.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.40.28191"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2009.00194.x"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.97.16.9098"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.177.14.4121-4130.1995"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/28.22.e97"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.120163297"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkh340"},{"key":"e_1_3_3_26_2","doi-asserted-by":"publisher","DOI":"10.1093\/sysbio\/syq010"},{"key":"e_1_3_3_27_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.05516-11"},{"key":"e_1_3_3_28_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.179.9.2857-2862.1997"},{"key":"e_1_3_3_29_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2011.07539.x"},{"key":"e_1_3_3_30_2","doi-asserted-by":"publisher","DOI":"10.1002\/bit.21375"},{"key":"e_1_3_3_31_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.145.1.657-660.1981"},{"key":"e_1_3_3_32_2","doi-asserted-by":"publisher","DOI":"10.1093\/genetics\/122.3.491"},{"key":"e_1_3_3_33_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.05052-11"},{"key":"e_1_3_3_34_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.181.18.5644-5651.1999"},{"key":"e_1_3_3_35_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0027475"},{"key":"e_1_3_3_36_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00055-12"},{"key":"e_1_3_3_37_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2011.07732.x"},{"key":"e_1_3_3_38_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.chembiol.2008.06.005"},{"key":"e_1_3_3_39_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.05383-11"},{"key":"e_1_3_3_40_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0606039103"},{"key":"e_1_3_3_41_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.177.14.4089-4096.1995"},{"key":"e_1_3_3_42_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.chembiol.2012.09.010"},{"key":"e_1_3_3_43_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2012.08173.x"},{"key":"e_1_3_3_44_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.02863-07"},{"key":"e_1_3_3_45_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.176.17.5341-5349.1994"},{"key":"e_1_3_3_46_2","doi-asserted-by":"publisher","DOI":"10.1111\/febs.12041"},{"key":"e_1_3_3_47_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00976-06"},{"key":"e_1_3_3_48_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00287-08"},{"key":"e_1_3_3_49_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2004.02.005"}],"container-title":["Journal of Bacteriology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.01361-13","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.01361-13","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T13:37:15Z","timestamp":1627565835000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/JB.01361-13"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,3,15]]},"references-count":48,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2014,3,15]]}},"alternative-id":["10.1128\/JB.01361-13"],"URL":"https:\/\/doi.org\/10.1128\/jb.01361-13","relation":{},"ISSN":["0021-9193","1098-5530"],"issn-type":[{"value":"0021-9193","type":"print"},{"value":"1098-5530","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,3,15]]},"assertion":[{"value":"2013-11-16","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2013-12-26","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2014-02-21","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}