{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T06:57:59Z","timestamp":1791269879678,"version":"4.1.0"},"reference-count":64,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2011,3,1]],"date-time":"2011-03-01T00:00:00Z","timestamp":1298937600000},"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":[[2011,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Despite the essential function of lipopolysaccharides (LPS) in Gram-negative bacteria, it is largely unknown how the exact amount of this molecule in the outer membrane is controlled. The first committed step in LPS biosynthesis is catalyzed by the LpxC enzyme. In\n            <jats:italic>Escherichia coli<\/jats:italic>\n            , the cellular concentration of LpxC is adjusted by the only essential protease in this organism, the membrane-anchored metalloprotease FtsH. Turnover of\n            <jats:italic>E. coli<\/jats:italic>\n            LpxC requires a length- and sequence-specific C-terminal degradation signal. LpxC proteins from\n            <jats:italic>Salmonella<\/jats:italic>\n            ,\n            <jats:italic>Yersinia<\/jats:italic>\n            , and\n            <jats:italic>Vibrio<\/jats:italic>\n            species carry similar C-terminal ends and, like the\n            <jats:italic>E. coli<\/jats:italic>\n            enzyme, were degraded by FtsH. Although LpxC proteins are highly conserved in Gram-negative bacteria, there are striking differences in their C termini. The\n            <jats:italic>Aquifex aeolicus<\/jats:italic>\n            enzyme, which is devoid of the C-terminal extension, was stable in\n            <jats:italic>E. coli<\/jats:italic>\n            , whereas LpxC from the alphaproteobacteria\n            <jats:italic>Agrobacterium tumefaciens<\/jats:italic>\n            and\n            <jats:italic>Rhodobacter capsulatus<\/jats:italic>\n            was degraded by the Lon protease. Proteolysis of the\n            <jats:italic>A. tumefaciens<\/jats:italic>\n            protein required the C-terminal end of LpxC. High stability of\n            <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n            LpxC in\n            <jats:italic>E. coli<\/jats:italic>\n            and\n            <jats:italic>P. aeruginosa<\/jats:italic>\n            suggested that\n            <jats:italic>Pseudomonas<\/jats:italic>\n            uses a proteolysis-independent strategy to control its LPS content. The differences in LpxC turnover along with previously reported differences in susceptibility against antimicrobial compounds have important implications for the potential of LpxC as a drug target.\n          <\/jats:p>","DOI":"10.1128\/jb.01043-10","type":"journal-article","created":{"date-parts":[[2010,12,31]],"date-time":"2010-12-31T03:43:31Z","timestamp":1293767011000},"page":"1090-1097","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":61,"title":["Control of Lipopolysaccharide Biosynthesis by FtsH-Mediated Proteolysis of LpxC Is Conserved in Enterobacteria but Not in All Gram-Negative Bacteria"],"prefix":"10.1128","volume":"193","author":[{"given":"Sina","family":"Langklotz","sequence":"first","affiliation":[{"name":"Lehrstuhl fu\u0308r Biologie der Mikroorganismen, Ruhr-Universita\u0308t Bochum, Bochum, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Scha\u0308kermann","sequence":"additional","affiliation":[{"name":"Lehrstuhl fu\u0308r Biologie der Mikroorganismen, Ruhr-Universita\u0308t Bochum, Bochum, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Franz","family":"Narberhaus","sequence":"additional","affiliation":[{"name":"Lehrstuhl fu\u0308r Biologie der Mikroorganismen, Ruhr-Universita\u0308t Bochum, Bochum, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/br.36.4.525-557.1972"},{"key":"e_1_3_3_3_2","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1007\/s12104-009-9201-5","volume":"4","year":"2010","unstructured":"Barb, A. W., L. Jiang, C. R. Raetz, and P. Zhou. 2010. Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240. Biomol. NMR Assign. 4:37-40.","journal-title":"Biomol. NMR Assign."},{"key":"e_1_3_3_4_2","doi-asserted-by":"crossref","first-page":"18433","DOI":"10.1073\/pnas.0709412104","volume":"104","year":"2007","unstructured":"Barb, A. W., L. Jiang, C. R. Raetz, and P. Zhou. 2007. Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: time-dependent inhibition and specificity in ligand binding. Proc. Natl. Acad. Sci. U. S. A. 104:18433-18438.","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"e_1_3_3_5_2","doi-asserted-by":"crossref","first-page":"3068","DOI":"10.1021\/bi900167q","volume":"48","year":"2009","unstructured":"Barb, A. W., et al. 2009. Uridine-based inhibitors as new leads for antibiotics targeting Escherichia coli LpxC. Biochemistry 48:3068-3077.","journal-title":"Biochemistry"},{"key":"e_1_3_3_6_2","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1111\/j.1365-2958.2007.05770.x","volume":"65","year":"2007","unstructured":"Barembruch, C., and R. Hengge. 2007. Cellular levels and activity of the flagellar sigma factor FliA of Escherichia coli are controlled by FlgM-modulated proteolysis. Mol. Microbiol. 65:76-89.","journal-title":"Mol. Microbiol."},{"key":"e_1_3_3_7_2","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1111\/j.1365-2958.2001.02313.x","volume":"39","year":"2001","unstructured":"Becker, G., and R. Hengge-Aronis. 2001. What makes an Escherichia coli promoter \u03c3S dependent? Role of the \u221213\/\u221214 nucleotide promoter positions and region 2.5 of \u03c3S. Mol. Microbiol. 39:1153-1165.","journal-title":"Mol. Microbiol."},{"key":"e_1_3_3_8_2","doi-asserted-by":"crossref","first-page":"9677","DOI":"10.1074\/jbc.274.14.9677","volume":"274","year":"1999","unstructured":"Carty, S. M., K. R. Sreekumar, and C. R. Raetz. 1999. Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction at 12 \u00b0C of an acyltransferase specific for palmitoleoyl-acyl carrier protein. J. Biol. Chem. 274:9677-9685.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_9_2","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/S0960-894X(98)00749-5","volume":"9","year":"1999","unstructured":"Chen, M. H., et al. 1999. Carbohydroxamido-oxazolidines: antibacterial agents that target lipid A biosynthesis. Bioorg. Med. Chem. Lett. 9:313-318.","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00860-07"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.46.6.1793-1799.2002"},{"key":"e_1_3_3_12_2","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1038\/32831","volume":"392","year":"1998","unstructured":"Deckert, G., et al. 1998. The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature 392:353-358.","journal-title":"Nature"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(94)35157-0"},{"key":"e_1_3_3_14_2","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1017\/S0016672300012593","volume":"18","year":"1971","unstructured":"Dunn, N. W., and B. W. Holloway. 1971. Pleiotrophy of p-fluorophenylalanine-resistant and antibiotic hypersensitive mutants of Pseudomonas aeruginosa. Genet. Res. 18:185-197.","journal-title":"Genet. Res."},{"key":"e_1_3_3_15_2","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1046\/j.1365-2958.2002.02887.x","volume":"44","year":"2002","unstructured":"Fischer, B., G. Rummel, P. Aldridge, and U. Jenal. 2002. The FtsH protease is involved in development, stress response and heat shock control in Caulobacter crescentus. Mol. Microbiol. 44:461-478.","journal-title":"Mol. Microbiol."},{"key":"e_1_3_3_16_2","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1111\/j.1365-2958.2005.04994.x","volume":"59","year":"2006","unstructured":"F\u00fchrer, F., S. Langklotz, and F. Narberhaus. 2006. The C-terminal end of LpxC is required for degradation by the FtsH protease. Mol. Microbiol. 59:1025-1036.","journal-title":"Mol. Microbiol."},{"key":"e_1_3_3_17_2","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.jmb.2007.06.083","volume":"372","year":"2007","unstructured":"F\u00fchrer, F., et al. 2007. Sequence and length recognition of the C-terminal turnover element of LpxC, a soluble substrate of the membrane-bound FtsH protease. J. Mol. Biol. 372:485-496.","journal-title":"J. Mol. Biol."},{"key":"e_1_3_3_18_2","doi-asserted-by":"crossref","first-page":"33788","DOI":"10.1074\/jbc.M110.147173","volume":"285","year":"2010","unstructured":"Gattis, S. G., M. Hernick, and C. A. Fierke. 2010. Active site metal ion in UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions. J. Biol. Chem. 285:33788-33796.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.28.3.1044-1047.1980"},{"key":"e_1_3_3_20_2","doi-asserted-by":"crossref","first-page":"7940","DOI":"10.1021\/bi060823m","volume":"45","year":"2006","unstructured":"Gennadios, H. A., D. A. Whittington, X. Li, C. A. Fierke, and D. W. Christianson. 2006. Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase. Biochemistry 45:7940-7948.","journal-title":"Biochemistry"},{"key":"e_1_3_3_21_2","doi-asserted-by":"crossref","first-page":"3889","DOI":"10.1101\/gad.12.24.3889","volume":"12","year":"1998","unstructured":"Gonzalez, M., E. G. Frank, A. S. Levine, and R. Woodgate. 1998. Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis. Genes Dev. 12:3889-3899.","journal-title":"Genes Dev."},{"key":"e_1_3_3_22_2","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.1101\/gad.12.9.1338","volume":"12","year":"1998","unstructured":"Gottesman, S., E. Roche, Y. Zhou, and R. T. Sauer. 1998. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12:1338-1347.","journal-title":"Genes Dev."},{"key":"e_1_3_3_23_2","first-page":"3","volume":"7","year":"2001","unstructured":"Gronow, S., and H. Brade. 2001. Lipopolysaccharide biosynthesis: which steps do bacteria need to survive? J. Endotoxin Res. 7:3-23.","journal-title":"J. Endotoxin Res."},{"key":"e_1_3_3_24_2","doi-asserted-by":"crossref","first-page":"16113","DOI":"10.1073\/pnas.0808802105","volume":"105","year":"2008","unstructured":"Gur, E., and R. T. Sauer. 2008. Evolution of the ssrA degradation tag in Mycoplasma: specificity switch to a different protease. Proc. Natl. Acad. Sci. U. S. A. 105:16113-16118.","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"e_1_3_3_25_2","doi-asserted-by":"crossref","first-page":"2267","DOI":"10.1101\/gad.1670908","volume":"22","year":"2008","unstructured":"Gur, E., and R. T. Sauer. 2008. Recognition of misfolded proteins by Lon, a AAA+ protease. Genes Dev. 22:2267-2277.","journal-title":"Genes Dev."},{"key":"e_1_3_3_26_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.177.14.4121-4130.1995"},{"key":"e_1_3_3_27_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.72.2.795-809.2004"},{"key":"e_1_3_3_28_2","doi-asserted-by":"publisher","DOI":"10.1038\/35020000"},{"key":"e_1_3_3_29_2","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.1101\/gad.12.9.1348","volume":"12","year":"1998","unstructured":"Herman, C., D. Th\u00e9venet, P. Bouloc, G. C. Walker, and R. D'Ari. 1998. Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH). Genes Dev. 12:1348-1355.","journal-title":"Genes Dev."},{"key":"e_1_3_3_30_2","doi-asserted-by":"crossref","first-page":"2246","DOI":"10.1021\/bi902066t","volume":"49","year":"2010","unstructured":"Hernick, M., S. G. Gattis, J. E. Penner-Hahn, and C. A. Fierke. 2010. Activation of Escherichia coli UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase by Fe2+ yields a more efficient enzyme with altered ligand affinity. Biochemistry 49:2246-2255.","journal-title":"Biochemistry"},{"key":"e_1_3_3_31_2","doi-asserted-by":"crossref","first-page":"11002","DOI":"10.1074\/jbc.275.15.11002","volume":"275","year":"2000","unstructured":"Jackman, J. E., et al. 2000. Antibacterial agents that target lipid A biosynthesis in gram-negative bacteria. Inhibition of diverse UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylases by substrate analogs containing zinc binding motifs. J. Biol. Chem. 275:11002-11009.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_32_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2036282100"},{"key":"e_1_3_3_33_2","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1021\/ci6004806","volume":"47","year":"2007","unstructured":"Kadam, R. U., A. V. Shivange, and N. Roy. 2007. Escherichia coli versus Pseudomonas aeruginosa deacetylase LpxC inhibitors selectivity: surface and cavity-depth-based analysis. J. Chem. Infect. Model. 47:1215-1224.","journal-title":"J. Chem. Infect. Model."},{"key":"e_1_3_3_34_2","doi-asserted-by":"crossref","first-page":"26225","DOI":"10.1074\/jbc.274.37.26225","volume":"274","year":"1999","unstructured":"Karata, K., T. Inagawa, A. J. Wilkinson, T. Tatsuta, and T. Ogura. 1999. Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH. J. Biol. Chem. 274:26225-26232.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_35_2","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/0003-2697(78)90260-9","volume":"85","year":"1978","unstructured":"Karkhanis, Y. D., J. Y. Zeltner, J. J. Jackson, and D. J. Carlo. 1978. A new and improved microassay to determine 2-keto-3-deoxyoctonate in lipopolysaccharide of Gram-negative bacteria. Anal. Biochem. 85:595-601.","journal-title":"Anal. Biochem."},{"key":"e_1_3_3_36_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00871-08"},{"key":"e_1_3_3_37_2","doi-asserted-by":"crossref","first-page":"3112","DOI":"10.1021\/jm010579r","volume":"45","year":"2002","unstructured":"Kline, T., et al. 2002. Potent, novel in vitro inhibitors of the Pseudomonas aeruginosa deacetylase LpxC. J. Med. Chem. 45:3112-3129.","journal-title":"J. Med. Chem."},{"key":"e_1_3_3_38_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.170.2.693-699.1988"},{"key":"e_1_3_3_39_2","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1177\/1087057109355319","volume":"15","year":"2010","unstructured":"Langsdorf, E. F., et al. 2010. Screening for antibacterial inhibitors of the UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) using a high-throughput mass spectrometry assay. J. Biomol. Screen. 15:52-61.","journal-title":"J. Biomol. Screen."},{"key":"e_1_3_3_40_2","doi-asserted-by":"publisher","DOI":"10.1093\/bioinformatics\/btm404"},{"key":"e_1_3_3_41_2","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1101\/gr.3513905","volume":"15","year":"2005","unstructured":"Lewenza, S., et al. 2005. Construction of a mini-Tn5-luxCDABE mutant library in Pseudomonas aeruginosa PAO1: a tool for identifying differentially regulated genes. Genome Res. 15:583-589.","journal-title":"Genome Res."},{"key":"e_1_3_3_42_2","doi-asserted-by":"crossref","first-page":"16574","DOI":"10.1021\/bi0518186","volume":"44","year":"2005","unstructured":"McClerren, A. L., et al. 2005. A slow, tight-binding inhibitor of the zinc-dependent deacetylase LpxC of lipid A biosynthesis with antibiotic activity comparable to ciprofloxacin. Biochemistry 44:16574-16583.","journal-title":"Biochemistry"},{"key":"e_1_3_3_43_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.00140-06"},{"key":"e_1_3_3_44_2","doi-asserted-by":"crossref","first-page":"32896","DOI":"10.1016\/S0021-9258(20)30075-2","volume":"269","year":"1994","unstructured":"Mohan, S., T. Kelly, S. Eveland, C. Raetz, and M. Anderson. 1994. An Escherichia coli gene (fabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. J. Biol. Chem. 269:32896-32903.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_45_2","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1016\/j.resmic.2009.08.011","volume":"160","year":"2009","unstructured":"Narberhaus, F., M. Obrist, F. F\u00fchrer, and S. Langklotz. 2009. Degradation of cytoplasmic substrates by FtsH, a membrane-anchored protease with many talents. Res. Microbiol. 160:652-659.","journal-title":"Res. Microbiol."},{"key":"e_1_3_3_46_2","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1177\/0968051907079399","volume":"13","year":"2007","unstructured":"Newman, M. A., J. M. Dow, A. Molinaro, and M. Parrilli. 2007. Priming, induction and modulation of plant defence responses by bacterial lipopolysaccharides. J. Endotoxin Res. 13:69-84.","journal-title":"J. Endotoxin Res."},{"key":"e_1_3_3_47_2","doi-asserted-by":"publisher","DOI":"10.1128\/mr.49.1.1-32.1985"},{"key":"e_1_3_3_48_2","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1046\/j.1365-2958.1999.01221.x","volume":"31","year":"1999","unstructured":"Ogura, T., et al. 1999. Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli. Mol. Microbiol. 31:833-844.","journal-title":"Mol. Microbiol."},{"key":"e_1_3_3_49_2","doi-asserted-by":"crossref","first-page":"980","DOI":"10.1126\/science.274.5289.980","volume":"274","year":"1996","unstructured":"Onishi, H. R., et al. 1996. Antibacterial agents that inhibit lipid A biosynthesis. Science 274:980-982.","journal-title":"Science"},{"key":"e_1_3_3_50_2","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.ijmm.2007.03.006","volume":"297","year":"2007","unstructured":"Opal, S. M. 2007. The host response to endotoxin, antilipopolysaccharide strategies, and the management of severe sepsis. Int. J. Med. Microbiol. 297:365-377.","journal-title":"Int. J. Med. Microbiol."},{"key":"e_1_3_3_51_2","doi-asserted-by":"crossref","first-page":"4359","DOI":"10.1021\/jm020183v","volume":"45","year":"2002","unstructured":"Pirrung, M. C., et al. 2002. Inhibition of the antibacterial target UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC): isoxazoline zinc amidase inhibitors bearing diverse metal binding groups. J. Med. Chem. 45:4359-4370.","journal-title":"J. Med. Chem."},{"key":"e_1_3_3_52_2","doi-asserted-by":"crossref","first-page":"11222","DOI":"10.1074\/jbc.275.15.11222","volume":"275","year":"2000","unstructured":"Pl\u00f6tz, B. M., B. Lindner, K. O. Stetter, and O. Holst. 2000. Characterization of a novel lipid A containing d-galacturonic acid that replaces phosphate residues. The structure of the lipid A of the lipopolysaccharide from the hyperthermophilic bacterium Aquifex pyrophilus. J. Biol. Chem. 275:11222-11228.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_53_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.01369-08"},{"key":"e_1_3_3_54_2","doi-asserted-by":"crossref","first-page":"2119","DOI":"10.1099\/mic.0.2008\/017368-0","volume":"154","year":"2008","unstructured":"Qiu, D., V. M. Eisinger, N. E. Head, G. B. Pier, and H. D. Yu. 2008. ClpXP proteases positively regulate alginate overexpression and mucoid conversion in Pseudomonas aeruginosa. Microbiology 154:2119-2130.","journal-title":"Microbiology"},{"key":"e_1_3_3_55_2","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1146\/annurev.biochem.76.010307.145803","volume":"76","year":"2007","unstructured":"Raetz, C. R., C. M. Reynolds, M. S. Trent, and R. E. Bishop. 2007. Lipid A modification systems in gram-negative bacteria. Annu. Rev. Biochem. 76:295-329.","journal-title":"Annu. Rev. Biochem."},{"key":"e_1_3_3_56_2","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1146\/annurev.biochem.71.110601.135414","volume":"71","year":"2002","unstructured":"Raetz, C. R., and C. Whitfield. 2002. Lipopolysaccharide endotoxins. Annu. Rev. Biochem. 71:635-700.","journal-title":"Annu. Rev. Biochem."},{"key":"e_1_3_3_57_2","unstructured":"Molecular cloning: a laboratory manual 2001"},{"key":"e_1_3_3_58_2","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(90)85008-C"},{"key":"e_1_3_3_59_2","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1099\/mic.0.28657-0","volume":"152","year":"2006","unstructured":"Su, S., B. B. Stephens, G. Alexandre, and S. K. Farrand. 2006. Lon protease of the \u03b1-proteobacterium Agrobacterium tumefaciens is required for normal growth, cellular morphology and full virulence. Microbiology 152:1197-1207.","journal-title":"Microbiology"},{"key":"e_1_3_3_60_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.160.2.724-732.1984"},{"key":"e_1_3_3_61_2","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1046\/j.1365-2958.1998.01091.x","volume":"30","year":"1998","unstructured":"Tatsuta, T., et al. 1998. Heat shock regulation in the ftsH null mutant of Escherichia coli: dissection of stability and activity control mechanisms of \u03c332 in vivo. Mol. Microbiol. 30:583-593.","journal-title":"Mol. Microbiol."},{"key":"e_1_3_3_62_2","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1038\/252169a0","volume":"252","year":"1974","unstructured":"Van Larebeke, N., et al. 1974. Large plasmid in Agrobacterium tumefaciens essential for crown gall-inducing ability. Nature 252:169-170.","journal-title":"Nature"},{"key":"e_1_3_3_63_2","doi-asserted-by":"crossref","first-page":"8146","DOI":"10.1073\/pnas.1432990100","volume":"100","year":"2003","unstructured":"Whittington, D. A., K. M. Rusche, H. Shin, C. A. Fierke, and D. W. Christianson. 2003. Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis. Proc. Natl. Acad. Sci. U. S. A. 100:8146-8150.","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"e_1_3_3_64_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.183.13.3885-3889.2001"},{"key":"e_1_3_3_65_2","doi-asserted-by":"crossref","first-page":"30384","DOI":"10.1074\/jbc.270.51.30384","volume":"270","year":"1995","unstructured":"Young, K., et al. 1995. The envA permeability\/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. J. Biol. Chem. 270:30384-30391.","journal-title":"J. Biol. Chem."}],"container-title":["Journal of Bacteriology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.01043-10","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.01043-10","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T17:22:50Z","timestamp":1627579370000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/JB.01043-10"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,3]]},"references-count":64,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2011,3]]}},"alternative-id":["10.1128\/JB.01043-10"],"URL":"https:\/\/doi.org\/10.1128\/jb.01043-10","relation":{},"ISSN":["0021-9193","1098-5530"],"issn-type":[{"value":"0021-9193","type":"print"},{"value":"1098-5530","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,3]]},"assertion":[{"value":"2010-09-02","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2010-12-21","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2011-02-09","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}