메뉴 건너뛰기




Volumn 188, Issue 12, 2006, Pages 4169-4182

Structural classification of bacterial response regulators: Diversity of output domains and domain combinations

Author keywords

[No Author keywords available]

Indexed keywords

ARAC PROTEIN; DNA BINDING PROTEIN; FACTOR FOR INVERSION STIMULATION; MERR PROTEIN; OUTER MEMBRANE PROTEIN REGULATOR; PROTEIN LYTTR; PROTEIN NARL; PROTEIN NTRC; PROTEIN RPOE; PROTEIN SPO0A; PROTEIN YCBB; UNCLASSIFIED DRUG;

EID: 33744983969     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01887-05     Document Type: Article
Times cited : (391)

References (157)
  • 1
    • 0032896914 scopus 로고    scopus 로고
    • Cell cycle-dependent degradation of a flagellar motor component requires a novel-type response regulator
    • Aldridge, P., and U. Jenal. 1999. Cell cycle-dependent degradation of a flagellar motor component requires a novel-type response regulator. Mol. Microbiol. 32:379-391.
    • (1999) Mol. Microbiol. , vol.32 , pp. 379-391
    • Aldridge, P.1    Jenal, U.2
  • 2
    • 0037346498 scopus 로고    scopus 로고
    • Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus
    • Aldridge, P., R. Paul, P. Goymer, P. Rainey, and U. Jenal. 2003. Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus. Mol. Microbiol. 47:1695-1708.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1695-1708
    • Aldridge, P.1    Paul, R.2    Goymer, P.3    Rainey, P.4    Jenal, U.5
  • 4
    • 30344469912 scopus 로고    scopus 로고
    • PilZ domain is part of the bacterial c-di-GMP binding protein
    • Amikam, D., and M. Y. Galperin. 2006. PilZ domain is part of the bacterial c-di-GMP binding protein. Bioinformatics 22:3-6.
    • (2006) Bioinformatics , vol.22 , pp. 3-6
    • Amikam, D.1    Galperin, M.Y.2
  • 5
    • 0032491213 scopus 로고    scopus 로고
    • Activation of methylesterase CheB: Evidence of a dual role for the regulatory domain
    • Anand, G. S., P. N. Goudreau, and A. M. Stock. 1998. Activation of methylesterase CheB: evidence of a dual role for the regulatory domain. Biochemistry 37:14038-14047.
    • (1998) Biochemistry , vol.37 , pp. 14038-14047
    • Anand, G.S.1    Goudreau, P.N.2    Stock, A.M.3
  • 6
    • 0037188414 scopus 로고    scopus 로고
    • Kinetic basis for the stimulatory effect of phosphorylation on the methylesterase activity of CheB
    • Anand, G. S., and A. M. Stock. 2002. Kinetic basis for the stimulatory effect of phosphorylation on the methylesterase activity of CheB. Biochemistry 41:6752-6760.
    • (2002) Biochemistry , vol.41 , pp. 6752-6760
    • Anand, G.S.1    Stock, A.M.2
  • 7
    • 0036529621 scopus 로고    scopus 로고
    • Comparative genomics and evolution of proteins involved in RNA metabolism
    • Anantharaman, V., E. V. Koonin, and L. Aravind. 2002. Comparative genomics and evolution of proteins involved in RNA metabolism. Nucleic Acids Res. 30:1427-1464.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1427-1464
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 8
    • 15944379232 scopus 로고    scopus 로고
    • The many faces of the helix-turn-helix domain: Transcription regulation and beyond
    • Aravind, L., V. Anantharaman, S. Balaji, M. M. Babu, and L. M. Iyer. 2005. The many faces of the helix-turn-helix domain: transcription regulation and beyond. FEMS Microbiol. Rev. 29:231-262.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 231-262
    • Aravind, L.1    Anantharaman, V.2    Balaji, S.3    Babu, M.M.4    Iyer, L.M.5
  • 9
    • 0032408864 scopus 로고    scopus 로고
    • The HD domain defines a new superfamily of metal-dependent phosphohydrolases
    • Aravind, L., and E. V. Koonin. 1998. The HD domain defines a new superfamily of metal-dependent phosphohydrolases. Trends Biochem. Sci. 23:469-472.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 469-472
    • Aravind, L.1    Koonin, E.V.2
  • 10
    • 0033277365 scopus 로고    scopus 로고
    • Bacterial tactic responses
    • Armitage, J. P. 1999. Bacterial tactic responses. Adv. Microb. Physiol. 41:229-289.
    • (1999) Adv. Microb. Physiol. , vol.41 , pp. 229-289
    • Armitage, J.P.1
  • 11
    • 1342279429 scopus 로고    scopus 로고
    • Survey of the number of two-component response regulator genes in the complete and annotated genome sequences of prokaryotes
    • Ashby, M. K. 2004. Survey of the number of two-component response regulator genes in the complete and annotated genome sequences of prokaryotes. FEMS Microbiol. Lett. 231:277-281.
    • (2004) FEMS Microbiol. Lett. , vol.231 , pp. 277-281
    • Ashby, M.K.1
  • 16
    • 20344396840 scopus 로고    scopus 로고
    • Archaeal transcriptional regulation-variation on a bacterial theme?
    • Bell, S. D. 2005. Archaeal transcriptional regulation-variation on a bacterial theme? Trends Microbiol. 13:262-265.
    • (2005) Trends Microbiol. , vol.13 , pp. 262-265
    • Bell, S.D.1
  • 17
    • 20344393380 scopus 로고    scopus 로고
    • Involvement of a Che-like signal transduction cascade in regulating cyst cell development in Rhodospirillum centenum
    • Berleman, J. E., and C. E. Bauer. 2005. Involvement of a Che-like signal transduction cascade in regulating cyst cell development in Rhodospirillum centenum. Mol. Microbiol. 56:1457-1466.
    • (2005) Mol. Microbiol. , vol.56 , pp. 1457-1466
    • Berleman, J.E.1    Bauer, C.E.2
  • 18
    • 0035912777 scopus 로고    scopus 로고
    • Light regulation of type IV pilus-dependent motility by chemosensor-like elements in Synechocystis PCC6803
    • Bhaya, D., A. Takahashi, and A. R. Grossman. 2001. Light regulation of type IV pilus-dependent motility by chemosensor-like elements in Synechocystis PCC6803. Proc. Natl. Acad. Sci. USA 98:7540-7545.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7540-7545
    • Bhaya, D.1    Takahashi, A.2    Grossman, A.R.3
  • 19
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • Bilwes, A. M., L. A. Alex, B. R. Crane, and M. I. Simon. 1999. Structure of CheA, a signal-transducing histidine kinase. Cell 96:131-141.
    • (1999) Cell , vol.96 , pp. 131-141
    • Bilwes, A.M.1    Alex, L.A.2    Crane, B.R.3    Simon, M.I.4
  • 20
    • 2442715070 scopus 로고    scopus 로고
    • Systematic insertional mutagenesis of a streptomycete genome: A link between osmoadaptation and antibiotic production
    • Bishop, A., S. Fielding, P. Dyson, and P. Herron. 2004. Systematic insertional mutagenesis of a streptomycete genome: a link between osmoadaptation and antibiotic production. Genome Res. 14:893-900.
    • (2004) Genome Res. , vol.14 , pp. 893-900
    • Bishop, A.1    Fielding, S.2    Dyson, P.3    Herron, P.4
  • 21
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • Blatch, G. L., and M. Lassle. 1999. The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. Bioessays 21:932-939.
    • (1999) Bioessays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lassle, M.2
  • 22
    • 20444385050 scopus 로고    scopus 로고
    • The phosphodiesterase activity of the HmsP EAL domain is required for negative regulation of biofilm formation in Yersinia pestis
    • Bobrov, A. G., O. Kirillina, and R. D. Perry. 2005. The phosphodiesterase activity of the HmsP EAL domain is required for negative regulation of biofilm formation in Yersinia pestis. FEMS Microbiol. Lett. 247:123-130.
    • (2005) FEMS Microbiol. Lett. , vol.247 , pp. 123-130
    • Bobrov, A.G.1    Kirillina, O.2    Perry, R.D.3
  • 23
    • 0036723852 scopus 로고    scopus 로고
    • R391: A conjugative integrating mosaic comprised of phage, plasmid, and transposon elements
    • Boltner, D., C. MacMahon, J. T. Pembroke, P. Strike, and A. M. Osborn. 2002. R391: a conjugative integrating mosaic comprised of phage, plasmid, and transposon elements. J. Bacteriol. 184:5158-5169.
    • (2002) J. Bacteriol. , vol.184 , pp. 5158-5169
    • Boltner, D.1    MacMahon, C.2    Pembroke, J.T.3    Strike, P.4    Osborn, A.M.5
  • 24
    • 0032496388 scopus 로고    scopus 로고
    • The N terminus of the flagellar switch protein, FliM, is the binding domain for the chemotactic response regulator, CheY
    • Bren, A., and M. Eisenbach. 1998. The N terminus of the flagellar switch protein, FliM, is the binding domain for the chemotactic response regulator, CheY. J. Mol. Biol. 278:507-514.
    • (1998) J. Mol. Biol. , vol.278 , pp. 507-514
    • Bren, A.1    Eisenbach, M.2
  • 27
    • 0029914578 scopus 로고    scopus 로고
    • The devR gene product is characteristic of receivers of two-component regulatory systems and is essential for heterocyst development in the filamentous cyanobacterium Nostoc sp. strain ATCC 29133
    • Campbell, E. L., K. D. Hagen, M. F. Cohen, M. L. Summers, and J. C. Meeks. 1996. The devR gene product is characteristic of receivers of two-component regulatory systems and is essential for heterocyst development in the filamentous cyanobacterium Nostoc sp. strain ATCC 29133. J. Bacteriol. 178:2037-2043.
    • (1996) J. Bacteriol. , vol.178 , pp. 2037-2043
    • Campbell, E.L.1    Hagen, K.D.2    Cohen, M.F.3    Summers, M.L.4    Meeks, J.C.5
  • 30
    • 24744457756 scopus 로고    scopus 로고
    • Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP
    • Christen, M., B. Christen, M. Folcher, A. Schauerte, and U. Jenal. 2005. Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP. J. Biol. Chem. 280:30829-30837.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30829-30837
    • Christen, M.1    Christen, B.2    Folcher, M.3    Schauerte, A.4    Jenal, U.5
  • 32
    • 0030465532 scopus 로고    scopus 로고
    • Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 Å resolution
    • Das, A. K., N. R. Helps, P. T. Cohen, and D. Barford. 1996. Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 Å resolution. EMBO J. 15:6798-6809.
    • (1996) EMBO J. , vol.15 , pp. 6798-6809
    • Das, A.K.1    Helps, N.R.2    Cohen, P.T.3    Barford, D.4
  • 33
    • 0035148589 scopus 로고    scopus 로고
    • Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: Crystal structure of the type II beta regulatory subunit
    • Diller, T. C., Madhusudan, N. H. Xuong, and S. S. Taylor. 2001. Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: crystal structure of the type II beta regulatory subunit. Structure 9:73-82.
    • (2001) Structure , vol.9 , pp. 73-82
    • Diller, T.C.1    Madhusudan2    Xuong, N.H.3    Taylor, S.S.4
  • 34
    • 0032539671 scopus 로고    scopus 로고
    • Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain
    • Djordjevic, S., P. N. Goudreau, Q. Xu, A. M. Stock, and A. H. West. 1998. Structural basis for methylesterase CheB regulation by a phosphorylation- activated domain. Proc. Natl. Acad. Sci. USA 95:1381-1386.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1381-1386
    • Djordjevic, S.1    Goudreau, P.N.2    Xu, Q.3    Stock, A.M.4    West, A.H.5
  • 35
    • 0021984180 scopus 로고
    • DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the dye and OmpR proteins
    • Drury, L. S., and R. S. Buxton. 1985. DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the dye and OmpR proteins. J. Biol. Chem. 260:4236-4242.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4236-4242
    • Drury, L.S.1    Buxton, R.S.2
  • 36
    • 0027976503 scopus 로고
    • PrrA, a putative response regulator involved in oxygen regulation of photosynthesis gene expression in Rhodobacter sphaeroides
    • Eraso, J. M., and S. Kaplan. 1994. PrrA, a putative response regulator involved in oxygen regulation of photosynthesis gene expression in Rhodobacter sphaeroides. J. Bacteriol. 176:32-43.
    • (1994) J. Bacteriol. , vol.176 , pp. 32-43
    • Eraso, J.M.1    Kaplan, S.2
  • 37
    • 0032911313 scopus 로고    scopus 로고
    • Two-component signal transduction in Bacillus subtilis: How one organism sees its world
    • Fabret, C., V. A. Feher, and J. A. Hoch. 1999. Two-component signal transduction in Bacillus subtilis: how one organism sees its world. J. Bacteriol. 181:1975-1983.
    • (1999) J. Bacteriol. , vol.181 , pp. 1975-1983
    • Fabret, C.1    Feher, V.A.2    Hoch, J.A.3
  • 38
    • 2642573619 scopus 로고    scopus 로고
    • Using genomic context in the analysis of multi-component systems
    • M. Y. Galperin and E. V. Koonin (ed.). Caister Academic Press, Wymondham, United Kingdom
    • Fedorova, N. D., A. N. Nikolskaya, and M. Y. Galperin. 2003. Using genomic context in the analysis of multi-component systems, p. 167-194. In M. Y. Galperin and E. V. Koonin (ed.). Frontiers in computational genomics, vol. 3. Caister Academic Press, Wymondham, United Kingdom.
    • (2003) Frontiers in Computational Genomics , vol.3 , pp. 167-194
    • Fedorova, N.D.1    Nikolskaya, A.N.2    Galperin, M.Y.3
  • 40
    • 0028270395 scopus 로고
    • D-dependent gene encodes a novel protein with both CheW and CheY homologous domains
    • D-dependent gene encodes a novel protein with both CheW and CheY homologous domains. J. Bacteriol. 176:2727-2735.
    • (1994) J. Bacteriol. , vol.176 , pp. 2727-2735
    • Fredrick, K.L.1    Helmann, J.D.2
  • 41
    • 2642554922 scopus 로고    scopus 로고
    • Bacterial signal transduction network in a genomic perspective
    • Galperin, M. Y. 2004. Bacterial signal transduction network in a genomic perspective. Environ. Microbiol. 6:552-567.
    • (2004) Environ. Microbiol. , vol.6 , pp. 552-567
    • Galperin, M.Y.1
  • 42
    • 23944523895 scopus 로고    scopus 로고
    • A census of membrane-bound and intracellular signal transduction proteins in bacteria: Bacterial IQ, extroverts and introverts
    • Online
    • Galperin, M. Y. 2005. A census of membrane-bound and intracellular signal transduction proteins in bacteria: bacterial IQ, extroverts and introverts. BMC Microbiol. 5:35. [Online.] http://www.biomedcentral.com/1471-2180/5/35.
    • (2005) BMC Microbiol. , vol.5 , pp. 35
    • Galperin, M.Y.1
  • 43
    • 33745004743 scopus 로고    scopus 로고
    • Bacterial signal transduction modules: From genomics to biology
    • Galperin, M. Y., and M. Gomelsky. 2005. Bacterial signal transduction modules: from genomics to biology. ASM News 71:326-333.
    • (2005) ASM News , vol.71 , pp. 326-333
    • Galperin, M.Y.1    Gomelsky, M.2
  • 44
    • 0035576329 scopus 로고    scopus 로고
    • Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes
    • Galperin, M. Y., and M. J. Jedrzejas. 2001. Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes. Proteins 45:318-324.
    • (2001) Proteins , vol.45 , pp. 318-324
    • Galperin, M.Y.1    Jedrzejas, M.J.2
  • 45
    • 0033222409 scopus 로고    scopus 로고
    • A specialized version of the HD hydrolase domain implicated in signal transduction
    • Galperin, M. Y., D. A. Natale, L. Aravind, and E. V. Koonin. 1999. A specialized version of the HD hydrolase domain implicated in signal transduction. J. Mol. Microbiol. Biotechnol. 1:303-305.
    • (1999) J. Mol. Microbiol. Biotechnol. , vol.1 , pp. 303-305
    • Galperin, M.Y.1    Natale, D.A.2    Aravind, L.3    Koonin, E.V.4
  • 46
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin, M. Y., A. N. Nikolskaya, and E. V. Koonin. 2001. Novel domains of the prokaryotic two-component signal transduction systems. FEMS Microbiol. Lett. 203:11-21.
    • (2001) FEMS Microbiol. Lett. , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 47
    • 20344386725 scopus 로고    scopus 로고
    • Archaeal transcription and its regulators
    • Geiduschek, E. P., and M. Ouhammouch. 2005. Archaeal transcription and its regulators. Mol. Microbiol. 56:1397-1407.
    • (2005) Mol. Microbiol. , vol.56 , pp. 1397-1407
    • Geiduschek, E.P.1    Ouhammouch, M.2
  • 48
    • 0033277340 scopus 로고    scopus 로고
    • The histidine protein kinase superfamily
    • Grebe, T. W., and J. B. Stock. 1999. The histidine protein kinase superfamily. Adv. Microb. Physiol. 41:139-227.
    • (1999) Adv. Microb. Physiol. , vol.41 , pp. 139-227
    • Grebe, T.W.1    Stock, J.B.2
  • 49
    • 0034982114 scopus 로고    scopus 로고
    • Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP
    • Green, J., C. Scott, and J. R. Guest. 2001. Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP. Adv. Microb. Physiol. 44:1-34.
    • (2001) Adv. Microb. Physiol. , vol.44 , pp. 1-34
    • Green, J.1    Scott, C.2    Guest, J.R.3
  • 50
    • 18244362812 scopus 로고    scopus 로고
    • Solution structure of the carbon storage regulator protein CsrA from Escherichia coli
    • Gutierrez, P., Y. Li, M. J. Osborne, E. Pomerantseva, Q. Liu, and K. Gehring. 2005. Solution structure of the carbon storage regulator protein CsrA from Escherichia coli. J. Bacteriol. 187:3496-3501.
    • (2005) J. Bacteriol. , vol.187 , pp. 3496-3501
    • Gutierrez, P.1    Li, Y.2    Osborne, M.J.3    Pomerantseva, E.4    Liu, Q.5    Gehring, K.6
  • 51
    • 4143110958 scopus 로고    scopus 로고
    • Genome-wide comparison of the His-to-Asp phosphorelay signaling components of three symbiotic genera of Rhizobia
    • Hagiwara, D., T. Yamashino, and T. Mizuno. 2004. Genome-wide comparison of the His-to-Asp phosphorelay signaling components of three symbiotic genera of Rhizobia. DNA Res. 11:57-65.
    • (2004) DNA Res. , vol.11 , pp. 57-65
    • Hagiwara, D.1    Yamashino, T.2    Mizuno, T.3
  • 52
    • 0028844985 scopus 로고
    • Identification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentus
    • Hecht, G. B., and A. Newton. 1995. Identification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentus. J. Bacteriol. 177:6223-6229.
    • (1995) J. Bacteriol. , vol.177 , pp. 6223-6229
    • Hecht, G.B.1    Newton, A.2
  • 54
    • 0034676026 scopus 로고    scopus 로고
    • Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor
    • Ho, Y. S., L. M. Burden, and J. H. Hurley. 2000. Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor. EMBO J. 19:5288-5299.
    • (2000) EMBO J. , vol.19 , pp. 5288-5299
    • Ho, Y.S.1    Burden, L.M.2    Hurley, J.H.3
  • 55
    • 0003438040 scopus 로고
    • Hoch, J. A., and T. J. Silhavy (ed.). ASM Press, Washington, D.C.
    • Hoch, J. A., and T. J. Silhavy (ed.). 1995. Two-component signal transduction. ASM Press, Washington, D.C.
    • (1995) Two-component Signal Transduction
  • 56
    • 1342325451 scopus 로고    scopus 로고
    • Transcriptional profiling of Caulobacter crescentus during growth on complex and minimal media
    • Hottes, A. K., M. Meewan, D. Yang, N. Arana, P. Romero, H. H. McAdams, and C. Stephens. 2004. Transcriptional profiling of Caulobacter crescentus during growth on complex and minimal media. J. Bacteriol. 186:1448-1461.
    • (2004) J. Bacteriol. , vol.186 , pp. 1448-1461
    • Hottes, A.K.1    Meewan, M.2    Yang, D.3    Arana, N.4    Romero, P.5    McAdams, H.H.6    Stephens, C.7
  • 57
    • 0142038557 scopus 로고    scopus 로고
    • Inouye, M., and R. Dutta (ed.). Academic Press, San Diego, Calif.
    • Inouye, M., and R. Dutta (ed.). 2003. Histidine kinases in signal transduction. Academic Press, San Diego, Calif.
    • (2003) Histidine Kinases in Signal Transduction
  • 58
    • 1842610464 scopus 로고    scopus 로고
    • Cyclic di-guanosine-monophosphate comes of age: A novel secondary messenger involved in modulating cell surface structures in bacteria?
    • Jenal, U. 2004. Cyclic di-guanosine-monophosphate comes of age: a novel secondary messenger involved in modulating cell surface structures in bacteria? Curr. Opin. Microbiol. 7:185-191.
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 185-191
    • Jenal, U.1
  • 59
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 61
    • 0035941366 scopus 로고    scopus 로고
    • Phosphorylation of the response regulator CheV is required for adaptation to attractants during Bacillus subtilis chemotaxis
    • Karatan, E., M. M. Saulmon, M. W. Bunn, and G. W. Ordal. 2001. Phosphorylation of the response regulator CheV is required for adaptation to attractants during Bacillus subtilis chemotaxis. J. Biol. Chem. 276:43618-43626.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43618-43626
    • Karatan, E.1    Saulmon, M.M.2    Bunn, M.W.3    Ordal, G.W.4
  • 62
    • 0347854362 scopus 로고    scopus 로고
    • The HWE histidine kinases, a new family of bacterial two-component sensor kinases with potentially diverse roles in environmental signaling
    • Karniol, B., and R. D. Vierstra. 2004. The HWE histidine kinases, a new family of bacterial two-component sensor kinases with potentially diverse roles in environmental signaling. J. Bacteriol. 186:445-453.
    • (2004) J. Bacteriol. , vol.186 , pp. 445-453
    • Karniol, B.1    Vierstra, R.D.2
  • 63
    • 0030940479 scopus 로고    scopus 로고
    • Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB
    • Kato, M., T. Mizuno, T. Shimizu, and T. Hakoshima. 1997. Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB. Cell 88:717-723.
    • (1997) Cell , vol.88 , pp. 717-723
    • Kato, M.1    Mizuno, T.2    Shimizu, T.3    Hakoshima, T.4
  • 64
    • 0037005989 scopus 로고    scopus 로고
    • Protein kinases and protein phosphatases in prokaryotes: A genomic perspective
    • Kennelly, P. J. 2002. Protein kinases and protein phosphatases in prokaryotes: a genomic perspective. FEMS Microbiol. Lett. 206:1-8.
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 1-8
    • Kennelly, P.J.1
  • 65
    • 0033599026 scopus 로고    scopus 로고
    • Structure of a transiently phosphorylated switch in bacterial signal transduction
    • Kern, D., B. F. Volkman, P. Luginbuhl, M. J. Nohaile, S. Kustu, and D. E. Wemmer. 1999. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature 402:894-898.
    • (1999) Nature , vol.402 , pp. 894-898
    • Kern, D.1    Volkman, B.F.2    Luginbuhl, P.3    Nohaile, M.J.4    Kustu, S.5    Wemmer, D.E.6
  • 66
    • 0035019043 scopus 로고    scopus 로고
    • Genomic analysis of the histidine kinase family in bacteria and archaea
    • Kim, D., and S. Forst. 2001. Genomic analysis of the histidine kinase family in bacteria and archaea. Microbiology 147:1197-1212.
    • (2001) Microbiology , vol.147 , pp. 1197-1212
    • Kim, D.1    Forst, S.2
  • 67
    • 0028122355 scopus 로고
    • The major dimerization determinants of the nitrogen regulatory protein NtrC from enteric bacteria lie in its carboxy-terminal domain
    • Klose, K. E., A. K. North, K. M. Stedman, and S. Kustu. 1994. The major dimerization determinants of the nitrogen regulatory protein NtrC from enteric bacteria lie in its carboxy-terminal domain. J. Mol. Biol. 241:233-245.
    • (1994) J. Mol. Biol. , vol.241 , pp. 233-245
    • Klose, K.E.1    North, A.K.2    Stedman, K.M.3    Kustu, S.4
  • 68
    • 1542327668 scopus 로고    scopus 로고
    • Trends between gene content and genome size in prokaryotic species with larger genomes
    • Konstantinidis, K. T., and J. M. Tiedje. 2004. Trends between gene content and genome size in prokaryotic species with larger genomes. Proc. Natl. Acad. Sci. USA 101:3160-3165.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3160-3165
    • Konstantinidis, K.T.1    Tiedje, J.M.2
  • 69
    • 0001938035 scopus 로고    scopus 로고
    • A comparative-genomic view of the microbial stress response
    • G. Storz and R. Hengge-Aronis (ed.). ASM Press, Washington, D.C.
    • Koonin, E. V., L. Aravind, and M. Y. Galperin. 2000. A comparative-genomic view of the microbial stress response, p. 417-444. In G. Storz and R. Hengge-Aronis (ed.), Bacterial stress responses. ASM Press, Washington, D.C.
    • (2000) Bacterial Stress Responses , pp. 417-444
    • Koonin, E.V.1    Aravind, L.2    Galperin, M.Y.3
  • 73
    • 0344237366 scopus 로고    scopus 로고
    • Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: Insights into DNA binding specificity
    • Laguri, C., M. K. Phillips-Jones, and M. P. Williamson. 2003. Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificity. Nucleic Acids Res. 31:6778-6787.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6778-6787
    • Laguri, C.1    Phillips-Jones, M.K.2    Williamson, M.P.3
  • 74
    • 0032854781 scopus 로고    scopus 로고
    • Domain organization and molecular characterization of 13 two-component systems identified by genome sequencing of Streptococcus pneumoniae
    • Lange, R., C. Wagner, A. de Saizieu, N. Flint, J. Molnos, M. Stieger, P. Caspers, M. Kamber, W. Keck, and K. E. Amrein. 1999. Domain organization and molecular characterization of 13 two-component systems identified by genome sequencing of Streptococcus pneumoniae. Gene 237:223-234.
    • (1999) Gene , vol.237 , pp. 223-234
    • Lange, R.1    Wagner, C.2    De Saizieu, A.3    Flint, N.4    Molnos, J.5    Stieger, M.6    Caspers, P.7    Kamber, M.8    Keck, W.9    Amrein, K.E.10
  • 75
    • 0035844214 scopus 로고    scopus 로고
    • Crystal structure of activated CheY. Comparison with other activated receiver domains
    • Lee, S. Y., H. S. Cho, J. G. Pelton, D. Yan, E. A. Berry, and D. E. Wemmer. 2001. Crystal structure of activated CheY. Comparison with other activated receiver domains. J. Biol. Chem. 276:16425-16431.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16425-16431
    • Lee, S.Y.1    Cho, H.S.2    Pelton, J.G.3    Yan, D.4    Berry, E.A.5    Wemmer, D.E.6
  • 76
    • 0142091549 scopus 로고    scopus 로고
    • Regulation of the transcriptional activator NtrCl: Structural studies of the regulatory and AAA+ ATPase domains
    • Lee, S. Y., A. De La Torre, D. Yan, S. Kustu, B. T. Nixon, and D. E. Wemmer. 2003. Regulation of the transcriptional activator NtrCl: structural studies of the regulatory and AAA+ ATPase domains. Genes Dev. 17:2552-2563.
    • (2003) Genes Dev. , vol.17 , pp. 2552-2563
    • Lee, S.Y.1    De La Torre, A.2    Yan, D.3    Kustu, S.4    Nixon, B.T.5    Wemmer, D.E.6
  • 77
    • 13444281991 scopus 로고    scopus 로고
    • Bacterial chromosome segregation: Structure and DNA binding of the Soj dimer - A conserved biological switch
    • Leonard, T. A., P. J. Butler, and J. Lowe. 2005. Bacterial chromosome segregation: structure and DNA binding of the Soj dimer-a conserved biological switch. EMBO J. 24:270-282.
    • (2005) EMBO J. , vol.24 , pp. 270-282
    • Leonard, T.A.1    Butler, P.J.2    Lowe, J.3
  • 80
    • 0026647940 scopus 로고
    • The patA gene product, which contains a region similar to CheY of Escherichia coli, controls heterocyst pattern formation in the cyanobacterium Anabaena 7120
    • Liang, J., L. Scappino, and R. Haselkorn. 1992. The patA gene product, which contains a region similar to CheY of Escherichia coli, controls heterocyst pattern formation in the cyanobacterium Anabaena 7120. Proc. Natl. Acad. Sci. USA 89:5655-5659.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5655-5659
    • Liang, J.1    Scappino, L.2    Haselkorn, R.3
  • 81
    • 0024347198 scopus 로고
    • Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis
    • Lupas, A., and J. Stock. 1989. Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis. J. Biol. Chem. 264:17337-17342.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17337-17342
    • Lupas, A.1    Stock, J.2
  • 82
    • 0036428610 scopus 로고    scopus 로고
    • Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes
    • Madec, E., A. Laszkiewicz, A. Iwanicki, M. Obuchowski, and S. Seror. 2002. Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes. Mol. Microbiol. 46:571-586.
    • (2002) Mol. Microbiol. , vol.46 , pp. 571-586
    • Madec, E.1    Laszkiewicz, A.2    Iwanicki, A.3    Obuchowski, M.4    Seror, S.5
  • 83
    • 85142186686 scopus 로고    scopus 로고
    • Cyanobacterial response regulator PatA contains a conserved N-terminal domain (PATAN) with an alpha-helical insertion
    • 16 March, posting date. doi:10.1093/bioinformatics/bt1096
    • Makarova, K. S., E. V. Koonin, R. Haselkorn, and M. Y. Galperin. 16 March 2006, posting date. Cyanobacterial response regulator PatA contains a conserved N-terminal domain (PATAN) with an alpha-helical insertion. Bioinformatics [Online.] doi:10.1093/bioinformatics/bt1096.
    • (2006) Bioinformatics [Online]
    • Makarova, K.S.1    Koonin, E.V.2    Haselkorn, R.3    Galperin, M.Y.4
  • 86
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: Protein domain annotations on the fly
    • Marchler-Bauer, A., and S. H. Bryant. 2004. CD-Search: protein domain annotations on the fly. Nucleic Acids Res. 32:W327-W331.
    • (2004) Nucleic Acids Res. , vol.32
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 87
    • 0031568318 scopus 로고    scopus 로고
    • The DNA-binding domain of OmpR: Crystal structures of a winged helix transcription factor
    • Martinez-Hackert, E., and A. M. Stock. 1997. The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor. Structure 5:109-124.
    • (1997) Structure , vol.5 , pp. 109-124
    • Martinez-Hackert, E.1    Stock, A.M.2
  • 88
    • 0031566431 scopus 로고    scopus 로고
    • Structural relationships in the OmpR family of winged-helix transcription factors
    • Martinez-Hackert, E., and A. M. Stock. 1997. Structural relationships in the OmpR family of winged-helix transcription factors. J. Mol. Biol. 269:301-312.
    • (1997) J. Mol. Biol. , vol.269 , pp. 301-312
    • Martinez-Hackert, E.1    Stock, A.M.2
  • 89
    • 0021162488 scopus 로고
    • Overexpression and sequence of the Escherichia coli cheY gene and biochemical activities of the CheY protein
    • Matsumura, P., J. J. Rydel, R. Linzmeier, and D. Vacante. 1984. Overexpression and sequence of the Escherichia coli cheY gene and biochemical activities of the CheY protein. J. Bacteriol. 160:36-41.
    • (1984) J. Bacteriol. , vol.160 , pp. 36-41
    • Matsumura, P.1    Rydel, J.J.2    Linzmeier, R.3    Vacante, D.4
  • 90
    • 0031589010 scopus 로고    scopus 로고
    • Compilation of all genes encoding two-component phosphotransfer signal transducers in the genome of Escherichia coli
    • Mizuno, T. 1997. Compilation of all genes encoding two-component phosphotransfer signal transducers in the genome of Escherichia coli. DNA Res. 4:161-168.
    • (1997) DNA Res. , vol.4 , pp. 161-168
    • Mizuno, T.1
  • 91
    • 0030608407 scopus 로고    scopus 로고
    • Compilation of all genes encoding bacterial two-component signal transducers in the genome of the cyanobacterium, Synechocystis sp. strain PCC 6803
    • Mizuno, T., T. Kaneko, and S. Tabata. 1996. Compilation of all genes encoding bacterial two-component signal transducers in the genome of the cyanobacterium, Synechocystis sp. strain PCC 6803. DNA Res. 3:407-414.
    • (1996) DNA Res. , vol.3 , pp. 407-414
    • Mizuno, T.1    Kaneko, T.2    Tabata, S.3
  • 93
    • 0344406163 scopus 로고    scopus 로고
    • Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: Unusual combination of two subunit forms and molecular bases for causing and changing DNA bend
    • Muraoka, S., R. Okumura, N. Ogawa, T. Nonaka, K. Miyashita, and T. Senda. 2003. Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend. J. Mol. Biol. 328:555-566.
    • (2003) J. Mol. Biol. , vol.328 , pp. 555-566
    • Muraoka, S.1    Okumura, R.2    Ogawa, N.3    Nonaka, T.4    Miyashita, K.5    Senda, T.6
  • 94
    • 0036606155 scopus 로고    scopus 로고
    • A novel type of conserved DNA-binding domain in the transcriptional regulators of the AlgR/AgrA/LytR family
    • Nikolskaya, A. N., and M. Y. Galperin. 2002. A novel type of conserved DNA-binding domain in the transcriptional regulators of the AlgR/AgrA/LytR family. Nucleic Acids Res. 30:2453-2459.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2453-2459
    • Nikolskaya, A.N.1    Galperin, M.Y.2
  • 95
    • 0011559747 scopus 로고
    • Two-component regulatory systems responsive to environmental stimuli share strongly conserved domains with the nitrogen assimilation regulatory genes ntrB and ntrC
    • Nixon, B. T., C. W. Ronson, and F. M. Ausubel. 1986. Two-component regulatory systems responsive to environmental stimuli share strongly conserved domains with the nitrogen assimilation regulatory genes ntrB and ntrC. Proc. Natl. Acad. Sci. USA 83:7850-7854.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7850-7854
    • Nixon, B.T.1    Ronson, C.W.2    Ausubel, F.M.3
  • 96
    • 0033214785 scopus 로고    scopus 로고
    • Crystal structure and induction mechanism of AmiC-AmiR: A ligand-regulated transcription antitermination complex
    • O'Hara, B. P., R. A. Norman, P. T. Wan, S. M. Roe, T. E. Barrett, R. E. Drew, and L. H. Pearl. 1999. Crystal structure and induction mechanism of AmiC-AmiR: a ligand-regulated transcription antitermination complex. EMBO J. 18:5175-5186.
    • (1999) EMBO J. , vol.18 , pp. 5175-5186
    • O'Hara, B.P.1    Norman, R.A.2    Wan, P.T.3    Roe, S.M.4    Barrett, T.E.5    Drew, R.E.6    Pearl, L.H.7
  • 98
    • 8844239143 scopus 로고    scopus 로고
    • Structure and function of an unusual family of protein phosphatases: The bacterial chemotaxis proteins CheC and CheX
    • Park, S. Y., X. Chao, G. Gonzalez-Bonet, B. D. Beel, A. M. Bilwes, and B. R. Crane. 2004. Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX. Mol. Cell 16:563-574.
    • (2004) Mol. Cell , vol.16 , pp. 563-574
    • Park, S.Y.1    Chao, X.2    Gonzalez-Bonet, G.3    Beel, B.D.4    Bilwes, A.M.5    Crane, B.R.6
  • 99
    • 1842451699 scopus 로고    scopus 로고
    • Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain
    • Paul, R., S. Weiser, N. C. Amiot, C. Chan, T. Schirmer, B. Giese, and U. Jenal. 2004. Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain. Genes Dev. 18:715-727.
    • (2004) Genes Dev. , vol.18 , pp. 715-727
    • Paul, R.1    Weiser, S.2    Amiot, N.C.3    Chan, C.4    Schirmer, T.5    Giese, B.6    Jenal, U.7
  • 100
    • 0033536573 scopus 로고    scopus 로고
    • Solution structure of the DNA-binding domain of NtrC with three alanine substitutions
    • Pelton, J. G., S. Kustu, and D. E. Wemmer. 1999. Solution structure of the DNA-binding domain of NtrC with three alanine substitutions. J. Mol. Biol. 292:1095-1110.
    • (1999) J. Mol. Biol. , vol.292 , pp. 1095-1110
    • Pelton, J.G.1    Kustu, S.2    Wemmer, D.E.3
  • 101
    • 0028353302 scopus 로고
    • Cloning and nucleotide sequence of regA, a putative response regulator gene of Rhodobacter sphaeroides
    • Phillips-Jones, M. K., and C. N. Hunter. 1994. Cloning and nucleotide sequence of regA, a putative response regulator gene of Rhodobacter sphaeroides. FEMS Microbiol. Lett. 116:269-275.
    • (1994) FEMS Microbiol. Lett. , vol.116 , pp. 269-275
    • Phillips-Jones, M.K.1    Hunter, C.N.2
  • 102
    • 0035957004 scopus 로고    scopus 로고
    • Phylogeny of genes for secretion NTPases: Identification of the widespread tadA subfamily and development of a diagnostic key for gene classification
    • Planet, P. J., S. C. Kachlany, R. DeSalle, and D. H. Figurski. 2001. Phylogeny of genes for secretion NTPases: identification of the widespread tadA subfamily and development of a diagnostic key for gene classification. Proc. Natl. Acad. Sci. USA 98:2503-2508.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2503-2508
    • Planet, P.J.1    Kachlany, S.C.2    Desalle, R.3    Figurski, D.H.4
  • 103
    • 13444306641 scopus 로고    scopus 로고
    • NCBI Reference Sequence (RefSeq): A curated non-redundant sequence database of genomes, transcripts and proteins
    • Pruitt, K. D., T. Tatusova, and D. R. Maglott. 2005. NCBI Reference Sequence (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins. Nucleic Acids Res. 33:D501-D504.
    • (2005) Nucleic Acids Res. , vol.33
    • Pruitt, K.D.1    Tatusova, T.2    Maglott, D.R.3
  • 104
    • 7944221188 scopus 로고    scopus 로고
    • An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr protein phosphatase
    • Pullen, K. E., H. L. Ng, P. Y. Sung, M. C. Good, S. M. Smith, and T. Alber. 2004. An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr protein phosphatase. Structure 12:1947-1954.
    • (2004) Structure , vol.12 , pp. 1947-1954
    • Pullen, K.E.1    Ng, H.L.2    Sung, P.Y.3    Good, M.C.4    Smith, S.M.5    Alber, T.6
  • 105
    • 0028275819 scopus 로고
    • Isolation of Tn917 insertional mutants of Bacillus subtilis that are resistant to the protonophore carbonyl cyanide m-chlorophenylhydrazone
    • Quirk, P. G., A. A. Guffanti, S. Clejan, J. Cheng, and T. A. Krulwich. 1994. Isolation of Tn917 insertional mutants of Bacillus subtilis that are resistant to the protonophore carbonyl cyanide m-chlorophenylhydrazone. Biochim. Biophys. Acta 1186:27-34.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 27-34
    • Quirk, P.G.1    Guffanti, A.A.2    Clejan, S.3    Cheng, J.4    Krulwich, T.A.5
  • 106
    • 0032169864 scopus 로고    scopus 로고
    • A novel DNA-binding motif in MarA: The first structure for an AraC family transcriptional activator
    • Rhee, S., R. G. Martin, J. L. Rosner, and D. R. Davies. 1998. A novel DNA-binding motif in MarA: the first structure for an AraC family transcriptional activator. Proc. Natl. Acad. Sci. USA 95:10413-10418.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10413-10418
    • Rhee, S.1    Martin, R.G.2    Rosner, J.L.3    Davies, D.R.4
  • 107
    • 0038154011 scopus 로고    scopus 로고
    • Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily
    • Robinson, V. L., T. Wu, and A. M. Stock. 2003. Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily. J. Bacteriol. 185:4186-4194.
    • (2003) J. Bacteriol. , vol.185 , pp. 4186-4194
    • Robinson, V.L.1    Wu, T.2    Stock, A.M.3
  • 108
    • 0031697252 scopus 로고    scopus 로고
    • Global regulation by the small RNA-binding protein CsrA and the non-coding RNA molecule CsrB
    • Romeo, T. 1998. Global regulation by the small RNA-binding protein CsrA and the non-coding RNA molecule CsrB. Mol. Microbiol. 29:1321-1330.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1321-1330
    • Romeo, T.1
  • 109
    • 22644438480 scopus 로고    scopus 로고
    • C-di-GMP: The dawning of a novel bacterial signalling system
    • Römling, U., M. Gomelsky, and M. Y. Galperin. 2005. C-di-GMP: The dawning of a novel bacterial signalling system. Mol. Microbiol. 57:629-639.
    • (2005) Mol. Microbiol. , vol.57 , pp. 629-639
    • Römling, U.1    Gomelsky, M.2    Galperin, M.Y.3
  • 110
    • 0028333653 scopus 로고
    • Chemotaxis in Bacillus subtilis requires cither of two functionally redundant CheW homologs
    • Rosario, M. M., K. L. Fredrick, G. W. Ordal, and J. D. Helmann. 1994. Chemotaxis in Bacillus subtilis requires cither of two functionally redundant CheW homologs. J. Bacteriol. 176:2736-2739.
    • (1994) J. Bacteriol. , vol.176 , pp. 2736-2739
    • Rosario, M.M.1    Fredrick, K.L.2    Ordal, G.W.3    Helmann, J.D.4
  • 112
    • 14244254898 scopus 로고    scopus 로고
    • Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: Insights into biochemistry of the GGDEF protein domain
    • Ryjenkov, D. A., M. Tarutina, O. M. Moskvin, and M. Gomelsky. 2005. Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain. J. Bacteriol. 187:1792-1798.
    • (2005) J. Bacteriol. , vol.187 , pp. 1792-1798
    • Ryjenkov, D.A.1    Tarutina, M.2    Moskvin, O.M.3    Gomelsky, M.4
  • 113
    • 21844458141 scopus 로고    scopus 로고
    • Enhancement of glutamine utilization in Bacillus subtilis through the GlnK-GlnL two-component regulatory system
    • Satomura, T., D. Shimura, K. Asai, Y. Sadaie, K. Hirooka, and Y. Fujita. 2005. Enhancement of glutamine utilization in Bacillus subtilis through the GlnK-GlnL two-component regulatory system. J. Bacteriol. 187:4813-4821.
    • (2005) J. Bacteriol. , vol.187 , pp. 4813-4821
    • Satomura, T.1    Shimura, D.2    Asai, K.3    Sadaie, Y.4    Hirooka, K.5    Fujita, Y.6
  • 114
    • 21844451590 scopus 로고    scopus 로고
    • Ubiquitous protein domain EAL encodes cyclic diguanylate-specific phosphodiesterase: Enzymatically active and inactive EAL domains
    • Schmidt, A. J., D. A. Ryjenkov, and M. Gomelsky. 2005. Ubiquitous protein domain EAL encodes cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J. Bacteriol. 187:4774-4781.
    • (2005) J. Bacteriol. , vol.187 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 115
    • 0026585783 scopus 로고
    • Regulatory factors controlling photosynthetic reaction center and light-harvesting gene expression in Rhodobacter capsulants
    • Sganga, M. W., and C. E. Bauer. 1992. Regulatory factors controlling photosynthetic reaction center and light-harvesting gene expression in Rhodobacter capsulants. Cell 68:945-954.
    • (1992) Cell , vol.68 , pp. 945-954
    • Sganga, M.W.1    Bauer, C.E.2
  • 116
    • 2442687054 scopus 로고    scopus 로고
    • Manganese-dependent protein O-phosphatases in prokaryotes and their biological functions
    • Shi, L. 2004. Manganese-dependent protein O-phosphatases in prokaryotes and their biological functions. Front. Biosci. 9:1382-1397.
    • (2004) Front. Biosci. , vol.9 , pp. 1382-1397
    • Shi, L.1
  • 117
    • 0031764045 scopus 로고    scopus 로고
    • The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: A family portrait
    • Shi, L., M. Potts, and P. J. Kennelly. 1998. The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: a family portrait. FEMS Microbiol. Rev. 22:229-253.
    • (1998) FEMS Microbiol. Rev. , vol.22 , pp. 229-253
    • Shi, L.1    Potts, M.2    Kennelly, P.J.3
  • 119
    • 0036160325 scopus 로고    scopus 로고
    • ANTAR: An RNA-binding domain in transcription antitermination regulatory proteins
    • Shu, C. J., and I. B. Zhulin. 2002. ANTAR: an RNA-binding domain in transcription antitermination regulatory proteins. Trends Biochem. Sci. 27:3-5.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 3-5
    • Shu, C.J.1    Zhulin, I.B.2
  • 120
    • 0022405719 scopus 로고
    • Multiple forms of the CheB methylesterase in bacterial chemosensing
    • Simms, S. A., M. G. Keane, and J. Stock. 1985. Multiple forms of the CheB methylesterase in bacterial chemosensing. J. Biol. Chem. 260:10161-10168.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10161-10168
    • Simms, S.A.1    Keane, M.G.2    Stock, J.3
  • 121
    • 0034537739 scopus 로고    scopus 로고
    • A two-component system involving an HD-GYP domain protein links cell-cell signalling to pathogenicity gene expression in Xanthomonas campestris
    • Slater, H., A. Alvarez-Morales, C. E. Barber, M. J. Daniels, and J. M. Dow. 2000. A two-component system involving an HD-GYP domain protein links cell-cell signalling to pathogenicity gene expression in Xanthomonas campestris. Mol. Microbiol. 38:986-1003.
    • (2000) Mol. Microbiol. , vol.38 , pp. 986-1003
    • Slater, H.1    Alvarez-Morales, A.2    Barber, C.E.3    Daniels, M.J.4    Dow, J.M.5
  • 122
    • 0033659769 scopus 로고    scopus 로고
    • Control of sporulation initiation in Bacillus subtilis
    • Sonenshein, A. L. 2000. Control of sporulation initiation in Bacillus subtilis. Curr. Opin. Microbiol. 3:561-566.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 561-566
    • Sonenshein, A.L.1
  • 123
    • 15944418972 scopus 로고    scopus 로고
    • Molecular insights into the initiation of sporulation in gram-positive bacteria: New technologies for an old phenomenon
    • Stephenson, K., and R. J. Lewis. 2005. Molecular insights into the initiation of sporulation in gram-positive bacteria: new technologies for an old phenomenon. FEMS Microbiol. Rev. 29:281-301.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 281-301
    • Stephenson, K.1    Lewis, R.J.2
  • 124
    • 0022377092 scopus 로고
    • Homologies between the Salmonella typhimurium CheY protein and proteins involved in the regulation of chemotaxis, membrane protein synthesis, and sporulation
    • Stock, A., D. E. Koshland, Jr., and J. Stock. 1985. Homologies between the Salmonella typhimurium CheY protein and proteins involved in the regulation of chemotaxis, membrane protein synthesis, and sporulation. Proc. Natl. Acad. Sci. USA 82:7989-7993.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7989-7993
    • Stock, A.1    Koshland Jr., D.E.2    Stock, J.3
  • 126
    • 0024562159 scopus 로고
    • Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
    • Stock, A. M., J. M. Mottonen, J. B. Stock, and C. E. Schutt. 1989. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature 337:745-749.
    • (1989) Nature , vol.337 , pp. 745-749
    • Stock, A.M.1    Mottonen, J.M.2    Stock, J.B.3    Schutt, C.E.4
  • 128
    • 0036225822 scopus 로고    scopus 로고
    • Genetics of the phage growth limitation (Pgl) system of Streptomyces coelicolor A3(2)
    • Sumby, P., and M. C. Smith. 2002. Genetics of the phage growth limitation (Pgl) system of Streptomyces coelicolor A3(2). Mol. Microbiol. 44:489-500.
    • (2002) Mol. Microbiol. , vol.44 , pp. 489-500
    • Sumby, P.1    Smith, M.C.2
  • 129
    • 2542460079 scopus 로고    scopus 로고
    • Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade
    • Szurmant, H., T. J. Muff, and G. W. Ordal. 2004. Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade. J. Biol. Chem. 279:21787-21792.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21787-21792
    • Szurmant, H.1    Muff, T.J.2    Ordal, G.W.3
  • 130
    • 2942584862 scopus 로고    scopus 로고
    • Diversity in chemotaxis mechanisms among the bacteria and archaea
    • Szurmant, H., and G. W. Ordal. 2004. Diversity in chemotaxis mechanisms among the bacteria and archaea. Microbiol. Mol. Biol. Rev. 68:301-319.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 301-319
    • Szurmant, H.1    Ordal, G.W.2
  • 131
    • 25144489145 scopus 로고    scopus 로고
    • The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase
    • Tamayo, R., A. D. Tischler, and A. Camilli. 2005. The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase. J. Biol. Chem. 280:33324-33330.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33324-33330
    • Tamayo, R.1    Tischler, A.D.2    Camilli, A.3
  • 132
    • 3142721163 scopus 로고    scopus 로고
    • Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Tanaka, T., T. Fukui, S. Fujiwara, H. Atomi, and T. Imanaka. 2004. Concerted action of diacetylchitobiose deacetylase and exo-β-D- glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Biol. Chem. 279:30021-30027.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30021-30027
    • Tanaka, T.1    Fukui, T.2    Fujiwara, S.3    Atomi, H.4    Imanaka, T.5
  • 133
    • 0035824876 scopus 로고    scopus 로고
    • Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: A comparison with related NDP-sugar glycosyltransferases
    • Tarbouriech, N., S. J. Charnock, and G. J. Davies. 2001. Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar glycosyltransferases. J. Mol. Biol. 314:655-661.
    • (2001) J. Mol. Biol. , vol.314 , pp. 655-661
    • Tarbouriech, N.1    Charnock, S.J.2    Davies, G.J.3
  • 135
    • 0033956060 scopus 로고    scopus 로고
    • The COG database: A tool for genome-scale analysis of protein functions and evolution
    • Tatusov, R. L., M. Y. Galperin, D. A. Natale, and E. V. Koonin. 2000. The COG database: a tool for genome-scale analysis of protein functions and evolution. Nucleic Acids Res. 28:33-36.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 33-36
    • Tatusov, R.L.1    Galperin, M.Y.2    Natale, D.A.3    Koonin, E.V.4
  • 136
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B. L., and I. B. Zhulin. 1999. PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63:479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 137
    • 3843069972 scopus 로고    scopus 로고
    • Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation
    • Tischler, A. D., and A. Cantilli. 2004. Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation. Mol. Microbiol. 53:857-869.
    • (2004) Mol. Microbiol. , vol.53 , pp. 857-869
    • Tischler, A.D.1    Cantilli, A.2
  • 138
    • 0342557053 scopus 로고
    • Deduced product of the stage 0 sporulation gene spo0F shares homology with the Spo0A, OmpR, and SfrA proteins
    • Trach, K. A., J. W. Chapman, P. J. Piggot, and J. A. Hoch. 1985. Deduced product of the stage 0 sporulation gene spo0F shares homology with the Spo0A, OmpR, and SfrA proteins. Proc. Natl. Acad. Sci. USA 82:7260-7264.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7260-7264
    • Trach, K.A.1    Chapman, J.W.2    Piggot, P.J.3    Hoch, J.A.4
  • 139
    • 0028344267 scopus 로고
    • Alp suppression of Lon: Dependence on the slpA gene
    • Trempy, J. E., J. E. Kirby, and S. Gottesman. 1994. Alp suppression of Lon: dependence on the slpA gene. J. Bacteriol. 176:2061-2067.
    • (1994) J. Bacteriol. , vol.176 , pp. 2061-2067
    • Trempy, J.E.1    Kirby, J.E.2    Gottesman, S.3
  • 141
    • 12944325784 scopus 로고    scopus 로고
    • One-component systems dominate signal transduction in prokaryotes
    • Ulrich, L. E., E. V. Koonin, and I. B. Zhulin. 2005. One-component systems dominate signal transduction in prokaryotes. Trends Microbiol. 13:52-56.
    • (2005) Trends Microbiol. , vol.13 , pp. 52-56
    • Ulrich, L.E.1    Koonin, E.V.2    Zhulin, I.B.3
  • 142
    • 0041828241 scopus 로고    scopus 로고
    • Scaling laws in the functional content of genomes
    • van Nimwegen, E. 2003. Scaling laws in the functional content of genomes. Trends Genet. 19:479-484.
    • (2003) Trends Genet. , vol.19 , pp. 479-484
    • Van Nimwegen, E.1
  • 144
    • 3042590307 scopus 로고    scopus 로고
    • The Che4 pathway of Myxococcus xanthus regulates type IV pilus-mediated motility
    • Vlamakis, H. C., J. R. Kirby, and D. R. Zusman. 2004. The Che4 pathway of Myxococcus xanthus regulates type IV pilus-mediated motility. Mol. Microbiol. 52:1799-1811.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1799-1811
    • Vlamakis, H.C.1    Kirby, J.R.2    Zusman, D.R.3
  • 145
    • 0028927334 scopus 로고
    • Three-dimensional solution structure of the N-terminal receiver domain of NtrC
    • Volkman, B. F., M. J. Nohaile, N. K. Amy, S. Kustu, and D. E. Wemmer. 1995. Three-dimensional solution structure of the N-terminal receiver domain of NtrC. Biochemistry 34:1413-1424.
    • (1995) Biochemistry , vol.34 , pp. 1413-1424
    • Volkman, B.F.1    Nohaile, M.J.2    Amy, N.K.3    Kustu, S.4    Wemmer, D.E.5
  • 146
    • 0027366420 scopus 로고
    • Structural conservation in the CheY superfamily
    • Volz, K. 1993. Structural conservation in the CheY superfamily. Biochemistry 32:11741-11753.
    • (1993) Biochemistry , vol.32 , pp. 11741-11753
    • Volz, K.1
  • 147
    • 0025741662 scopus 로고
    • Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
    • Volz, K., and P. Matsumura. 1991. Crystal structure of Escherichia coli CheY refined at 1.7-A resolution. J. Biol. Chem. 266:15511-15519.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15511-15519
    • Volz, K.1    Matsumura, P.2
  • 148
    • 0037126659 scopus 로고    scopus 로고
    • Genomic analysis of protein kinases, protein phosphatases and two-component regulatory systems of the cyanobacterium Anabaena sp. strain PCC 7120
    • Wang, L., Y. P. Sun, W. L. Chen, J. H. Li, and C. C. Zhang. 2002. Genomic analysis of protein kinases, protein phosphatases and two-component regulatory systems of the cyanobacterium Anabaena sp. strain PCC 7120. FEMS Microbiol. Lett. 217:155-165.
    • (2002) FEMS Microbiol. Lett. , vol.217 , pp. 155-165
    • Wang, L.1    Sun, Y.P.2    Chen, W.L.3    Li, J.H.4    Zhang, C.C.5
  • 149
    • 0027517812 scopus 로고
    • Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria
    • Welch, M., K. Oosawa, S. Aizawa, and M. Eisenbach. 1993. Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc. Natl. Acad. Sci. USA 90:8787-8791.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8787-8791
    • Welch, M.1    Oosawa, K.2    Aizawa, S.3    Eisenbach, M.4
  • 150
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • West, A. H., and A. M. Stock. 2001. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 26:369-376.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 152
    • 0030929313 scopus 로고    scopus 로고
    • A novel family of proteins that regulates antibiotic production in streptomycetes appears to contain an OmpR-like DNA-binding fold
    • Wietzorrek, A., and M. Bibb. 1997. A novel family of proteins that regulates antibiotic production in streptomycetes appears to contain an OmpR-like DNA-binding fold. Mol. Microbiol. 25:1181-1184.
    • (1997) Mol. Microbiol. , vol.25 , pp. 1181-1184
    • Wietzorrek, A.1    Bibb, M.2
  • 153
    • 10144255829 scopus 로고    scopus 로고
    • Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor
    • Yang, X., C. M. Kang, M. S. Brody, and C. W. Price. 1996. Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor. Genes Dev. 10:2265-2275.
    • (1996) Genes Dev. , vol.10 , pp. 2265-2275
    • Yang, X.1    Kang, C.M.2    Brody, M.S.3    Price, C.W.4
  • 154
    • 2942733563 scopus 로고    scopus 로고
    • New knowledge from old: In silico discovery of novel protein domains in Streptomyces coelicolor
    • 6 February, posting date. [Online.] doi:10.1186/1471-2180-3-3
    • Yeats, C., S. Bentley, and A. Bateman. 6 February 2003, posting date. New knowledge from old: in silico discovery of novel protein domains in Streptomyces coelicolor. BMC Microbiol. 3:3. [Online.] doi:10.1186/1471-2180-3- 3.
    • (2003) BMC Microbiol. , vol.3 , pp. 3
    • Yeats, C.1    Bentley, S.2    Bateman, A.3
  • 155
    • 22144480660 scopus 로고    scopus 로고
    • HxlR, a member of the DUF24 protein family, is a DNA-binding protein that acts as a positive regulator of the formaldehyde-inducible hxlAB operon in Bacillus subtilis
    • Yurimoto, H., R. Hirai, N. Matsuno, H. Yasueda, N. Kato, and Y. Sakai. 2005. HxlR, a member of the DUF24 protein family, is a DNA-binding protein that acts as a positive regulator of the formaldehyde-inducible hxlAB operon in Bacillus subtilis. Mol. Microbiol. 57:511-519.
    • (2005) Mol. Microbiol. , vol.57 , pp. 511-519
    • Yurimoto, H.1    Hirai, R.2    Matsuno, N.3    Yasueda, H.4    Kato, N.5    Sakai, Y.6
  • 156
    • 0030901637 scopus 로고    scopus 로고
    • Structure of the adenylyl cyclase catalytic core
    • Zhang, G., Y. Liu, A. E. Ruoho, and J. H. Hurley. 1997. Structure of the adenylyl cyclase catalytic core. Nature 386:247-253.
    • (1997) Nature , vol.386 , pp. 247-253
    • Zhang, G.1    Liu, Y.2    Ruoho, A.E.3    Hurley, J.H.4
  • 157
    • 0037215715 scopus 로고    scopus 로고
    • Common extracellular sensory domains in transmembrane receptors for diverse signal transduction pathways in bacteria and archaea
    • Zhulin, I. B., A. N. Nikolskaya, and M. Y. Galperin. 2003. Common extracellular sensory domains in transmembrane receptors for diverse signal transduction pathways in bacteria and archaea. J. Bacteriol. 185:285-294.
    • (2003) J. Bacteriol. , vol.185 , pp. 285-294
    • Zhulin, I.B.1    Nikolskaya, A.N.2    Galperin, M.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.