J. S. Parkinson and E. C. Kofoid, Communication Modules in Bacterial Signaling Proteins, Annual Review of Genetics, vol.26, issue.1, pp.71-112, 1992.

D. Burbulys, K. A. Trach, and J. A. Hoch, Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay, Cell, vol.64, issue.3, pp.545-552, 1991.

J. L. Appleby, J. S. Parkinson, and R. B. Bourret, Signal Transduction via the Multi-Step Phosphorelay: Not Necessarily a Road Less Traveled, Cell, vol.86, issue.6, pp.845-848, 1996.

T. Mizuno, His-Asp Phosphotransfer Signal Transduction, Journal of Biochemistry, vol.123, issue.4, pp.555-563, 1998.

R. B. Bourret, J. Davagnino, and M. I. Simon, The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW., Journal of Bacteriology, vol.175, issue.7, pp.2097-2101, 1993.

T. B. Morrison and J. S. Parkinson, A fragment liberated from the Escherichia coli CheA kinase that blocks stimulatory, but not inhibitory, chemoreceptor signaling., Journal of bacteriology, vol.179, issue.17, pp.5543-5550, 1997.

H. Zhou and F. W. Dahlquist, Phosphotransfer Site of the Chemotaxis-Specific Protein Kinase CheA as Revealed by NMR?, Biochemistry, vol.36, issue.4, pp.699-710, 1997.

M. Kato, T. Mizuno, T. Shimizu, and T. Hakoshima, Insights into Multistep Phosphorelay from the Crystal Structure of the C-Terminal HPt Domain of ArcB, Cell, vol.88, issue.5, pp.717-723, 1997.

Q. Xu and A. H. West, Conservation of structure and function among histidine-containing phosphotransfer (HPt) domains as revealed by the crystal structure of YPD1 1 1Edited by I. A. Wilson, Journal of Molecular Biology, vol.292, issue.5, pp.1039-1050, 1999.

H. K. Song, J. Y. Lee, M. G. Lee, J. Moon, K. Min et al., Insights into eukaryotic multistep phosphorelay signal transduction revealed by the crystal structure of Ypd1p from Saccharomyces cerevisiae 1 1Edited by I. A. Wilson, Journal of Molecular Biology, vol.293, issue.4, pp.753-761, 1999.

T. Maeda, S. M. Wurgler-murphy, and H. Saito, A two-component system that regulates an osmosensing MAP kinase cascade in yeast, Nature, vol.369, issue.6477, pp.242-245, 1994.

C. Tomomori, T. Tanaka, R. Dutta, H. Park, S. K. Saha et al., SOLUTION STRUCTURE OF THE HOMODIMERIC DOMAIN OF ENVZ FROM ESCHERICHIA COLI BY MULTI-DIMENSIONAL NMR., Nat. Struct. Biol, vol.6, pp.729-734, 2000.

A. M. Bilwes, L. A. Alex, B. R. Crane, and M. I. Simon, CRYSTAL STRUCTURE OF CHEA-289, A SIGNAL TRANSDUCING HISTIDINE KINASE, Cell, vol.96, pp.131-141, 1999.

J. Wu, N. Ohta, J. Zhao, and A. Newton, A novel bacterial tyrosine kinase essential for cell division and differentiation, Proceedings of the National Academy of Sciences, vol.96, issue.23, pp.13068-13073, 1999.

K. I. Varughese, . Madhusudan, X. Z. Zhou, J. M. Whiteley, and J. A. Hoch, Formation of a Novel Four-Helix Bundle and Molecular Recognition Sites by Dimerization of a Response Regulator Phosphotransferase, Molecular Cell, vol.2, issue.4, pp.485-493, 1998.

T. Tanaka, S. K. Saha, C. Tomomori, R. Ishima, D. Liu et al., NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ, Nature, vol.396, issue.6706, pp.88-92, 1998.

C. Prodromou, S. M. Roe, R. O'brien, J. E. Ladbury, P. W. Piper et al., Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone, Cell, vol.90, issue.1, pp.65-75, 1997.

C. Ban and W. Yang, Crystal Structure and ATPase Activity of MutL, Cell, vol.95, issue.4, pp.541-552, 1998.

D. B. Wigley, G. J. Davies, E. J. Dodson, A. Maxwell, and G. Dodson, Crystal structure of an N-terminal fragment of the DNA gyrase B protein, Nature, vol.351, issue.6328, pp.624-629, 1991.

Y. Yang and M. Inouye, Requirement of Both Kinase and Phosphatase Activities of an Escherichia coli Receptor (Taz1) for Ligand-dependent Signal Transduction, Journal of Molecular Biology, vol.231, issue.2, pp.335-342, 1993.

R. C. Stewart, R. Vanbruggen, D. D. Ellefson, and A. J. Wolfe, TNP-ATP and TNP-ADP as Probes of the Nucleotide Binding Site of CheA, the Histidine Protein Kinase in the Chemotaxis Signal Transduction Pathway ofEscherichia coli?, Biochemistry, vol.37, issue.35, pp.12269-12279, 1998.

T. W. Grebe and J. B. Stock, The Histidine Protein Kinase Superfamily, Advances in Microbial Physiology, vol.41, pp.139-227, 1999.

I. M. Ota and A. Varshavsky, A yeast protein similar to bacterial two-component regulators, Science, vol.262, issue.5133, pp.566-569, 1993.

K. Min, C. M. Hilditch, B. Diederich, J. Errington, and M. D. Yudkin, ?F, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-? factor that is also a protein kinase, Cell, vol.74, issue.4, pp.735-742, 1993.

C. M. Kang, M. S. Brody, S. Akbar, X. Yang, and C. W. Price, Homologous pairs of regulatory proteins control activity of Bacillus subtilis transcription factor sigma(b) in response to environmental stress., Journal of bacteriology, vol.178, issue.13, pp.3846-3853, 1996.

S. M. Najafi, A. C. Willis, and M. D. Yudkin, Site of phosphorylation of SpoIIAA, the anti-anti-sigma factor for sporulation-specific sigma F of Bacillus subtilis., Journal of bacteriology, vol.177, issue.10, pp.2912-2913, 1995.

W. Hsing, F. D. Russo, K. K. Bernd, and T. J. Silhavy, Mutations That Alter the Kinase and Phosphatase Activities of the Two-Component Sensor EnvZ, Journal of Bacteriology, vol.180, issue.17, pp.4538-4546, 1998.

M. Foussard, S. Cabantous, J. Pédelacq, V. Guillet, S. Tranier et al., The molecular puzzle of two-component signaling cascades, Microbes and Infection, vol.3, issue.5, pp.417-424, 2001.
URL : https://hal.archives-ouvertes.fr/hal-03004328

T. Msadek, F. Kunst, and G. Rapoport, A Signal Transduction Network in Bacillus subtilis Includes the DegS/DegU and ComP/ComA Two-Component Systems, Two-Component Signal Transduction, pp.447-471, 2014.

M. Perego and J. A. Hoch, Protein aspartate phosphatases control the output of two-component signal transduction systems, Trends in Genetics, vol.12, issue.3, pp.97-101, 1996.

J. F. Hess, K. Oosawa, N. Kaplan, and M. I. Simon, Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis, Cell, vol.53, issue.1, pp.79-87, 1988.

D. Georgellis, O. Kwon, P. De-wulf, and E. C. Lin, Signal Decay through a Reverse Phosphorelay in the Arc Two-component Signal Transduction System, Journal of Biological Chemistry, vol.273, issue.49, pp.32864-32869, 1998.

V. Sourjik and R. Schmitt, Phosphotransfer between CheA, CheY1, and CheY2 in the Chemotaxis Signal Transduction Chain ofRhizobium meliloti?, Biochemistry, vol.37, issue.8, pp.2327-2335, 1998.

B. Gu, J. H. Lee, T. R. Hoover, D. Scholl, and B. T. Nixon, Rhizobium meliloti DctD, a ?54-dependent transcriptional activator, may be negatively controlled by a subdomain in the C-terminal end of its two-component receiver module, Molecular Microbiology, vol.13, issue.1, pp.51-66, 1994.

K. Ireton, D. Z. Rudner, K. J. Siranosian, and A. D. Grossman, Integration of multiple developmental signals in Bacillus subtilis through the Spo0A transcription factor., Genes & Development, vol.7, issue.2, pp.283-294, 1993.

D. Kahn and G. Ditta, Modular structure of Fix J: homology of the transcriptional activator domain with the -35 binding domain of sigma factors, Molecular Microbiology, vol.5, issue.4, pp.987-997, 1991.

I. Baikalov, I. Schröder, M. Kaczor-grzeskowiak, D. Cascio, R. P. Gunsalus et al., NarL Dimerization? Suggestive Evidence from a New Crystal Form?,?, Biochemistry, vol.37, issue.11, pp.3665-3676, 1998.

S. Djordjevic, P. N. Goudreau, Q. Xu, A. M. Stock, and A. H. West, STRUCTURAL BASIS FOR METHYLESTERASE CHEB REGULATION BY A PHOSPHORYLATION-ACTIVATED DOMAIN, Proc. Natl. Acad. Sci. USA, vol.95, pp.1381-1386, 1998.

M. A. Cervin and G. B. Spiegelman, The Spo0A sof mutations reveal regions of the regulatory domain that interact with a sensor kinase and RNA polymerase, Molecular Microbiology, vol.31, issue.2, pp.597-607, 1999.

R. J. Lewis, J. A. Brannigan, K. Muchova, I. Barak, and A. J. Wilkinson, Phosphorylated aspartate in the crystal structure of the sporulation response regulator, Spo0A, J. Mol. Biol, vol.294, pp.9-15, 1999.

C. Birck, L. Mourey, P. Gouet, B. Fabry, J. Schumacher et al., Conformational changes induced by phosphorylation of the FixJ receiver domain, Structure, vol.7, issue.12, pp.1505-1515, 1999.
URL : https://hal.archives-ouvertes.fr/hal-00314286

R. J. Lewis, K. Muchová, J. A. Brannigan, I. Barák, G. Leonard et al., Domain swapping in the sporulation response regulator Spo0A, Journal of Molecular Biology, vol.297, issue.3, pp.757-770, 2000.

P. Gouet, B. Fabry, V. Guillet, C. Birck, L. Mourey et al., Structural transitions in the FixJ receiver domain, Structure, vol.7, issue.12, pp.1517-1526, 1999.
URL : https://hal.archives-ouvertes.fr/hal-00428429

S. Da-re, J. Schumacher, P. Rousseau, J. Fourment, C. Ebel et al., Phosphorylation-induced dimerization of the FixJ receiver domain, Molecular Microbiology, vol.34, issue.3, pp.504-511, 1999.
URL : https://hal.archives-ouvertes.fr/hal-00428426

D. Yan, H. S. Cho, C. A. Hastings, M. M. Igo, S. Lee et al., Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators, Proceedings of the National Academy of Sciences, vol.96, issue.26, pp.14789-14794, 1999.

H. S. Cho, S. Y. Lee, D. Yan, X. Pan, J. S. Parkinson et al., SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI, J. Mol. Biol, vol.297, pp.543-551, 2000.

C. J. Halkides, M. M. Mcevoy, E. Casper, P. Matsumura, K. Volz et al., The 1.9 Å Resolution Crystal Structure of Phosphono-CheY, an Analogue of the Active Form of the Response Regulator, CheY?,?, Biochemistry, vol.39, issue.18, pp.5280-5286, 2000.

M. Welch, N. Chinardet, L. Mourey, C. Birck, and J. Samama, Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY, Nature Structural Biology, vol.5, issue.1, pp.25-29, 1998.
URL : https://hal.archives-ouvertes.fr/hal-03004494

J. Stock and S. Da-re, Signal transduction: Response regulators on and off, Current Biology, vol.10, issue.11, pp.R420-R424, 2000.

R. Novak, B. Henriques, E. Charpentier, S. Normark, and E. Tuomanen, Emergence of vancomycin tolerance in Streptococcus pneumoniae, Nature, vol.399, issue.6736, pp.590-593, 1999.

J. P. Throup, K. K. Koretke, A. P. Bryant, K. A. Ingraham, A. F. Chalker et al., A genomic analysis of two-component signal transduction in Streptococcus pneumoniae, Molecular Microbiology, vol.35, issue.3, pp.566-576, 2002.

E. G. Véscovi, F. C. Soncini, and E. A. Groisman, Mg2+ as an Extracellular Signal: Environmental Regulation of Salmonella Virulence, Cell, vol.84, issue.1, pp.165-174, 1996.

F. C. Soncini and E. A. Groisman, Two-component regulatory systems can interact to process multiple environmental signals., Journal of bacteriology, vol.178, issue.23, pp.6796-6801, 1996.

T. Shimizu, W. Ba-thein, M. Tamaki, and H. Hayashi, The virR gene, a member of a class of two-component response regulators, regulates the production of perfringolysin O, collagenase, and hemagglutinin in Clostridium perfringens., Journal of Bacteriology, vol.176, issue.6, pp.1616-1623, 1994.

R. Foussard, Foussard, Pierre, 2011.