A. B. Russell, S. B. Peterson, and J. D. Mougous, Type VI secretion system effectors: poisons with a purpose, Nature Reviews Microbiology, vol.8, issue.2, pp.137-148, 2014.
DOI : 10.1371/journal.pone.0057609
URL : http://europepmc.org/articles/pmc4256078?pdf=render

E. Durand, C. Cambillau, E. Cascales, and L. Journet, VgrG, Tae, Tle, and beyond: the versatile arsenal of Type VI secretion effectors, Trends in Microbiology, vol.22, issue.9, pp.498-507, 2014.
DOI : 10.1016/j.tim.2014.06.004
URL : https://hal.archives-ouvertes.fr/hal-01458195

A. Diniz, J. Liu, Y. C. Coulthurst, and S. J. , Molecular weaponry: diverse effectors delivered by the Type VI secretion system, Cellular Microbiology, vol.1843, issue.12, pp.1742-1751, 2015.
DOI : 10.1016/j.bbamcr.2014.03.018

A. Hachani, T. E. Wood, and A. Filloux, Type VI secretion and anti-host effectors, Current Opinion in Microbiology, vol.29, pp.81-93, 2015.
DOI : 10.1016/j.mib.2015.11.006

G. Bönemann, A. Pietrosiuk, and A. Mogk, Tubules and donuts: a type VI secretion story, Molecular Microbiology, vol.72, issue.4, pp.815-821, 2010.
DOI : 10.1099/00221287-139-4-859

E. Cascales and C. Cambillau, Structural biology of type VI secretion systems, Philosophical Transactions of the Royal Society B: Biological Sciences, vol.364, issue.2, pp.1102-1111, 2012.
DOI : 10.1016/j.jmb.2006.08.078
URL : https://hal.archives-ouvertes.fr/hal-01458261

S. J. Coulthurst, The Type VI secretion system ??? a widespread and versatile cell targeting system, Research in Microbiology, vol.164, issue.6, pp.640-654, 2013.
DOI : 10.1016/j.resmic.2013.03.017

A. Zoued, Y. R. Brunet, E. Durand, M. S. Aschtgen, L. Logger et al., Architecture and assembly of the Type VI secretion system, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol.1843, issue.8, pp.1664-1673, 2014.
DOI : 10.1016/j.bbamcr.2014.03.018
URL : https://hal.archives-ouvertes.fr/hal-01458220

S. Kube and P. Wendler, Structural comparison of contractile nanomachines, AIMS Biophysics, vol.2, issue.2, pp.88-115, 2015.
DOI : 10.3934/biophy.2015.2.88

M. Basler, Type VI secretion system: secretion by a contractile nanomachine, Philosophical Transactions of the Royal Society B: Biological Sciences, vol.55, issue.1679, p.1679, 2015.
DOI : 10.1128/JB.188.6.2254-2261.2006
URL : http://rstb.royalsocietypublishing.org/content/royptb/370/1679/20150021.full.pdf

B. T. Ho, T. G. Dong, and J. J. Mekalanos, A View to a Kill: The Bacterial Type VI Secretion System, Cell Host & Microbe, vol.15, issue.1, pp.9-21, 2014.
DOI : 10.1016/j.chom.2013.11.008

F. R. Cianfanelli, L. Monlezun, and S. J. Coulthurst, Aim, Load, Fire: The Type VI Secretion System, a Bacterial Nanoweapon, Trends in Microbiology, vol.24, issue.1, pp.51-62, 2016.
DOI : 10.1016/j.tim.2015.10.005

P. G. Leiman, M. Basler, U. A. Ramagopal, J. B. Bonanno, J. M. Sauder et al., Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin, Proceedings of the National Academy of Sciences, vol.25, issue.2, pp.4154-4159, 2009.
DOI : 10.1016/0022-2836(67)90136-2
URL : http://www.pnas.org/content/106/11/4154.full.pdf

M. Basler, M. Pilhofer, G. P. Henderson, G. J. Jensen, and J. J. Mekalanos, Type VI secretion requires a dynamic contractile phage tail-like structure, Nature, vol.1, issue.7388, pp.182-186, 2012.
DOI : 10.1038/nprot.2006.432
URL : http://europepmc.org/articles/pmc3527127?pdf=render

Y. R. Brunet, A. Zoued, F. Boyer, B. Douzi, and E. Cascales, The Type VI Secretion TssEFGK-VgrG Phage-Like Baseplate Is Recruited to the TssJLM Membrane Complex via Multiple Contacts and Serves As Assembly Platform for Tail Tube/Sheath Polymerization, PLOS Genetics, vol.43, issue.10, 2015.
DOI : 10.1371/journal.pgen.1005545.s005
URL : https://hal.archives-ouvertes.fr/hal-01778563

E. Durand, V. S. Nguyen, A. Zoued, L. Logger, G. Péhau-arnaudet et al., Biogenesis and structure of a type VI secretion membrane core complex, Nature, vol.508, issue.7562, pp.555-560, 2015.
DOI : 10.1038/nature13081
URL : https://hal.archives-ouvertes.fr/hal-01778556

E. R. Ballister, A. H. Lai, R. N. Zuckermann, Y. Cheng, and J. D. Mougous, In vitro self-assembly of tailorable nanotubes from a simple protein building block, Proceedings of the National Academy of Sciences, vol.116, issue.1, pp.3733-3738, 2008.
DOI : 10.1006/jsbi.1996.0030

Y. R. Brunet, J. Hénin, H. Celia, and E. Cascales, Type VI secretion and bacteriophage tail tubes share a common assembly pathway, EMBO reports, vol.15, issue.3, pp.315-321, 2014.
DOI : 10.1002/embr.201337936
URL : https://hal.archives-ouvertes.fr/hal-01458198

M. Kudryashev, R. Y. Wang, M. Brackmann, S. Scherer, T. Maier et al., Structure of the Type VI Secretion System Contractile Sheath, Cell, vol.160, issue.5, pp.952-962, 2015.
DOI : 10.1016/j.cell.2015.01.037

Y. R. Brunet, L. Espinosa, S. Harchouni, T. Mignot, and E. Cascales, Imaging Type VI Secretion-Mediated Bacterial Killing, Cell Reports, vol.3, issue.1, pp.36-41, 2013.
DOI : 10.1016/j.celrep.2012.11.027
URL : https://hal.archives-ouvertes.fr/hal-01458227

M. Basler, B. T. Ho, and J. J. Mekalanos, Tit-for-Tat: Type VI Secretion System Counterattack during Bacterial Cell-Cell Interactions, Cell, vol.152, issue.4, pp.884-894, 2013.
DOI : 10.1016/j.cell.2013.01.042
URL : https://doi.org/10.1016/j.cell.2013.01.042

A. Zoued, E. Durand, Y. R. Brunet, S. Spinelli, B. Douzi et al., Priming and polymerization of a bacterial contractile tail structure, Nature, vol.9, issue.7592, pp.59-63, 2016.
DOI : 10.1371/journal.pone.0086918
URL : https://hal.archives-ouvertes.fr/hal-01439072

S. Pukatzki, A. T. Ma, A. T. Revel, D. Sturtevant, and J. J. Mekalanos, Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin, Proceedings of the National Academy of Sciences, vol.22, issue.22, pp.15508-15513, 2007.
DOI : 10.1093/nar/22.22.4673
URL : http://www.pnas.org/content/104/39/15508.full.pdf

A. Zoued, E. Durand, C. Bebeacua, Y. R. Brunet, B. Douzi et al., TssK Is a Trimeric Cytoplasmic Protein Interacting with Components of Both Phage-like and Membrane Anchoring Complexes of the Type VI Secretion System, Journal of Biological Chemistry, vol.12, issue.38, pp.27031-27041, 2013.
DOI : 10.1371/journal.pone.0067647
URL : https://hal.archives-ouvertes.fr/hal-01458230

G. English, O. Byron, F. R. Cianfanelli, A. R. Prescott, and S. J. Coulthurst, Biochemical analysis of TssK, a core component of the bacterial Type??VI secretion system, reveals distinct oligomeric states of TssK and identifies a TssK???TssFG subcomplex, Biochemical Journal, vol.461, issue.2, pp.291-304, 2014.
DOI : 10.1038/sj.emboj.7600409

N. M. Taylor, N. S. Prokhorov, R. C. Guerrero-ferreira, M. M. Shneider, C. Browning et al., Structure of the T4 baseplate and its function in triggering sheath contraction, Nature, vol.372, issue.7603, pp.346-352, 2016.
DOI : 10.1016/j.jmb.2007.05.022

S. Planamente, O. Salih, E. Manoli, D. Albesa-jové, P. S. Freemont et al., TssA forms a gp6???like ring attached to the type VI secretion sheath, The EMBO Journal, vol.35, issue.15, 2016.
DOI : 10.15252/embj.201694024

M. S. Aschtgen, C. S. Bernard, S. De-bentzmann, R. Lloubès, and E. Cascales, SciN Is an Outer Membrane Lipoprotein Required for Type VI Secretion in Enteroaggregative Escherichia coli, Journal of Bacteriology, vol.190, issue.22, pp.7523-7531, 2008.
DOI : 10.1128/JB.00945-08

L. S. Ma, J. S. Lin, and E. M. Lai, An IcmF Family Protein, ImpLM, Is an Integral Inner Membrane Protein Interacting with ImpKL, and Its Walker A Motif Is Required for Type VI Secretion System-Mediated Hcp Secretion in Agrobacterium tumefaciens, Journal of Bacteriology, vol.191, issue.13, pp.4316-4129, 2009.
DOI : 10.1128/JB.00029-09

M. S. Aschtgen, M. Gavioli, A. Dessen, R. Lloubès, and E. Cascales, Type VI secretion system to the cell wall, Molecular Microbiology, vol.66, issue.4, pp.886-899, 2010.
DOI : 10.1128/jb.174.24.7982-7988.1992

M. S. Aschtgen, A. Zoued, R. Lloubès, L. Journet, and E. Cascales, The C-tail anchored TssL subunit, an essential protein of the enteroaggregative Escherichia coli Sci-1 Type VI secretion system, is inserted by YidC, pp.71-82, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01458239

E. Durand, A. Zoued, S. Spinelli, P. J. Watson, M. S. Aschtgen et al., Structural Characterization and Oligomerization of the TssL Protein, a Component Shared by Bacterial Type VI and Type IVb Secretion Systems, Journal of Biological Chemistry, vol.40, issue.17, pp.14157-14168, 2012.
DOI : 10.1016/j.jmb.2007.05.022
URL : https://hal.archives-ouvertes.fr/hal-01458247

J. Zheng and K. Y. Leung, Dissection of a type VI secretion system in Edwardsiella tarda, Molecular Microbiology, vol.180, issue.5, 2007.
DOI : 10.1099/mic.0.2006/004952-0

C. Felisberto-rodrigues, E. Durand, M. S. Aschtgen, S. Blangy, M. Ortiz-lombardia et al., Towards a Structural Comprehension of Bacterial Type VI Secretion Systems: Characterization of the TssJ-TssM Complex of an Escherichia coli Pathovar, PLoS Pathogens, vol.15, issue.11, 2011.
DOI : 10.1371/journal.ppat.1002386.s010
URL : https://hal.archives-ouvertes.fr/hal-01458272

V. S. Nguyen, L. Logger, S. Spinelli, A. Desmyter, T. T. Le et al., Inhibition of Type VI Secretion by an Anti-TssM Llama Nanobody, PLOS ONE, vol.3, issue.3, 2015.
DOI : 10.1371/journal.pone.0122187.t002
URL : https://hal.archives-ouvertes.fr/hal-01217205

A. J. Gerc, A. Diepold, K. Trunk, M. Porter, C. Rickman et al., Visualization of the Serratia Type VI Secretion System Reveals Unprovoked Attacks and Dynamic Assembly, Cell Reports, vol.12, issue.12, pp.2131-2142, 2015.
DOI : 10.1016/j.celrep.2015.08.053

L. S. Ma, F. Narberhaus, and E. M. Lai, IcmF Family Protein TssM Exhibits ATPase Activity and Energizes Type VI Secretion, Journal of Biological Chemistry, vol.181, issue.19, pp.15610-15621, 2012.
DOI : 10.1126/science.290.5493.979
URL : http://www.jbc.org/content/287/19/15610.full.pdf

M. Bogdanov, W. Zhang, J. Xie, and W. Dowhan, Transmembrane protein topology mapping by the substituted cysteine accessibility method (SCAMTM): Application to lipid-specific membrane protein topogenesis, Methods, vol.36, issue.2, pp.148-171, 2005.
DOI : 10.1016/j.ymeth.2004.11.002

J. Söding, A. Biegert, and A. N. Lupas, The HHpred interactive server for protein homology detection and structure prediction, Nucleic Acids Research, vol.33, issue.Web Server, pp.244-248, 2005.
DOI : 10.1093/nar/gki408

I. Hanukoglu, Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide binding sites, Biochemistry and Molecular Biology Education, vol.43, issue.3, pp.206-209, 2015.
DOI : 10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-#
URL : http://onlinelibrary.wiley.com/doi/10.1002/bmb.20849/pdf

X. Wang, Z. Lou, X. Dong, W. Yang, Y. Peng et al., Crystal Structure of the C-Terminal Domain of Human DPY-30-Like Protein: A Component of the Histone Methyltransferase Complex, Journal of Molecular Biology, vol.390, issue.3, pp.530-537, 2009.
DOI : 10.1016/j.jmb.2009.05.061

N. Flaugnatti, T. T. Le, S. Canaan, M. S. Aschtgen, V. S. Nguyen et al., antibacterial Type VI secretion effector interacts directly with the C-terminal domain of the VgrG spike protein for delivery, Molecular Microbiology, vol.1843, issue.6, pp.1099-1118, 2016.
DOI : 10.1016/j.bbamcr.2014.04.022
URL : https://hal.archives-ouvertes.fr/hal-01778571

V. Tremblay, P. Zhang, C. P. Chaturvedi, J. Thornton, J. S. Brunzelle et al., Molecular Basis for DPY-30 Association to COMPASS-like and NURF Complexes, Structure, vol.22, issue.12, pp.1821-1830, 2014.
DOI : 10.1016/j.str.2014.10.002
URL : https://doi.org/10.1016/j.str.2014.10.002

V. A. Kostyuchenko, P. G. Leiman, P. R. Chipman, S. Kanamaru, M. J. Van-raaij et al., Three-dimensional structure of bacteriophage T4 baseplate, Nature Structural & Molecular Biology, vol.136, issue.9, pp.688-693, 2003.
DOI : 10.1006/jsbi.2002.4435

V. A. Kostyuchenko, P. R. Chipman, P. G. Leiman, F. Arisaka, V. V. Mesyanzhinov et al., The tail structure of bacteriophage T4 and its mechanism of contraction, Nature Structural & Molecular Biology, vol.125, issue.9, pp.810-813, 2005.
DOI : 10.1006/jsbi.1998.4080

P. G. Leiman, F. Arisaka, M. J. Van-raaij, V. A. Kostyuchenko, A. A. Aksyuk et al., Morphogenesis of the T4 tail and tail fibers, Virology Journal, vol.7, issue.1, p.355, 2010.
DOI : 10.1186/1743-422X-7-355

A. Paschos, A. Den-hartigh, M. A. Smith, V. L. Atluri, D. Sivanesan et al., ABSTRACT, Infection and Immunity, vol.79, issue.3, pp.1033-1043, 2011.
DOI : 10.1128/IAI.00993-10

M. A. Smith, M. Coinçon, A. Paschos, B. Jolicoeur, P. Lavallée et al., Identification of the Binding Site of Brucella VirB8 Interaction Inhibitors, Chemistry & Biology, vol.19, issue.8, pp.1041-1048, 2012.
DOI : 10.1016/j.chembiol.2012.07.007

A. Zaslaver, A. Bren, M. Ronen, S. Itzkovitz, I. Kikoin et al., A comprehensive library of fluorescent transcriptional reporters for Escherichia coli, Nature Methods, vol.297, issue.8, pp.623-628, 2006.
DOI : 10.1038/nmeth895

K. A. Datsenko and B. L. Wanner, One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products, Proceedings of the National Academy of Sciences, vol.27, issue.2, pp.6640-6645, 2000.
DOI : 10.1093/nar/27.2.389

M. K. Chaveroche, J. M. Ghigo, and C. Enfert, A rapid method for efficient gene replacement in the filamentous fungus Aspergillus nidulans, Nucleic Acids Research, vol.28, issue.22, p.97, 2000.
DOI : 10.1093/nar/28.22.e97

A. J. Link, D. Phillips, and G. M. Church, Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization., Journal of Bacteriology, vol.179, issue.20, pp.6228-6237, 1997.
DOI : 10.1128/jb.179.20.6228-6237.1997

A. Battesti and E. Bouveret, Acyl carrier protein/SpoT interaction, the switch linking SpoT-dependent stress response to fatty acid metabolism, Molecular Microbiology, vol.266, issue.4, pp.1048-1063, 2006.
DOI : 10.1128/JB.186.16.5249-5257.2004

Y. R. Brunet, C. S. Bernard, M. Gavioli, R. Lloubès, and E. Cascales, An Epigenetic Switch Involving Overlapping Fur and DNA Methylation Optimizes Expression of a Type VI Secretion Gene Cluster, PLoS Genetics, vol.66, issue.7, 2011.
DOI : 10.1371/journal.pgen.1002205.s002
URL : https://hal.archives-ouvertes.fr/hal-01458278

F. Van-den-ent and J. Löwe, RF cloning: A restriction-free method for inserting target genes into plasmids, Journal of Biochemical and Biophysical Methods, vol.67, issue.1, pp.67-74, 2006.
DOI : 10.1016/j.jbbm.2005.12.008

S. J. Jakubowski, V. Krishnamoorthy, E. Cascales, and P. J. Christie, Agrobacterium tumefaciens VirB6 Domains Direct the Ordered Export of a DNA Substrate Through a Type IV Secretion System, Journal of Molecular Biology, vol.341, issue.4, pp.961-977, 2004.
DOI : 10.1016/j.jmb.2004.06.052

E. L. Goemaere, A. Devert, R. Lloubès, and E. Cascales, Movements of the TolR C-terminal Domain Depend on TolQR Ionizable Key Residues and Regulate Activity of the Tol Complex, Journal of Biological Chemistry, vol.178, issue.24, pp.17749-17757, 2007.
DOI : 10.1128/jb.178.21.6116-6122.1996

G. Karimova, J. Pidoux, A. Ullmann, and D. Ladant, A bacterial two-hybrid system based on a reconstituted signal transduction pathway, Proceedings of the National Academy of Sciences, vol.16, issue.3, pp.5752-5756, 1998.
DOI : 10.1038/ng0797-277

A. Battesti and E. Bouveret, The bacterial two-hybrid system based on adenylate cyclase reconstitution in Escherichia coli, Methods, vol.58, issue.4, pp.325-334, 2012.
DOI : 10.1016/j.ymeth.2012.07.018
URL : https://hal.archives-ouvertes.fr/hal-01458246

G. E. Tusnády and I. Simon, Principles governing amino acid composition of integral membrane proteins: application to topology prediction 1 1Edited by J. Thornton, Journal of Molecular Biology, vol.283, issue.2, pp.489-506, 1998.
DOI : 10.1006/jmbi.1998.2107

A. Krogh, B. Larsson, G. Von-heijne, and E. L. Sonnhammer, Predicting transmembrane protein topology with a hidden markov model: application to complete genomes11Edited by F. Cohen, Journal of Molecular Biology, vol.305, issue.3, pp.567-580, 2001.
DOI : 10.1006/jmbi.2000.4315

K. Hofmann and W. Stoffel, A database of membrane spanning protein segments, Biol. Chem, vol.374, p.166, 1993.

B. Rost, P. Fariselli, and R. Casadio, Topology prediction for helical transmembrane proteins at 86% accuracy-Topology prediction at 86% accuracy, Protein Science, vol.227, issue.8, pp.1704-1718, 1996.
DOI : 10.1002/prot.340180309
URL : http://onlinelibrary.wiley.com/doi/10.1002/pro.5560050824/pdf

M. Biasini, S. Bienert, A. Waterhouse, K. Arnold, G. Studer et al., SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information, Nucleic Acids Research, vol.82, issue.Suppl. 2, pp.252-258, 2014.
DOI : 10.1002/prot.24347
URL : https://academic.oup.com/nar/article-pdf/42/W1/W252/7438166/gku340.pdf

E. F. Pettersen, T. D. Goddard, C. C. Huang, G. S. Couch, D. M. Greenblatt et al., UCSF Chimera?A visualization system for exploratory research and analysis, Journal of Computational Chemistry, vol.373, issue.13, pp.1605-1612, 2004.
DOI : 10.1002/jcc.20084
URL : http://www.cgl.ucsf.edu/home/tef/pubs/chimera.pdf

D. Tommaso, P. Moretti, S. Xenarios, I. Orobitg, M. Montanyola et al., T-Coffee: a web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension, Nucleic Acids Research, vol.26, issue.15, pp.13-17, 2011.
DOI : 10.1093/bioinformatics/btq304

A. Dereeper, V. Guignon, G. Blanc, S. Audic, S. Buffet et al., Phylogeny.fr: robust phylogenetic analysis for the non-specialist, Nucleic Acids Research, vol.21, issue.9, pp.465-469, 2008.
DOI : 10.1093/bioinformatics/bti263
URL : https://hal.archives-ouvertes.fr/lirmm-00324099

A. Zoued, C. J. Cassaro, E. Durand, B. Douzi, A. P. España et al., Structure???Function Analysis of the TssL Cytoplasmic Domain Reveals a New Interaction between the Type VI Secretion Baseplate and Membrane Complexes, Journal of Molecular Biology, vol.428, issue.22, 2016.
DOI : 10.1016/j.jmb.2016.08.030
URL : https://hal.archives-ouvertes.fr/hal-01439100