A. Battesti and E. Bouveret, Improvement of bacterial two-hybrid vectors for detection of fusion proteins and transfer to pBAD-tandem affinity purification, calmodulin binding peptide, or 6-histidine tag vectors, PROTEOMICS, vol.48, issue.22, pp.4768-71, 2008.
DOI : 10.1002/pmic.200800270

A. Battesti and E. Bouveret, The bacterial two-hybrid system based on adenylate cyclase reconstitution in Escherichia coli, Methods, vol.58, issue.4, pp.325-359, 2012.
DOI : 10.1016/j.ymeth.2012.07.018

URL : https://hal.archives-ouvertes.fr/hal-01458246

N. Bostanci and G. N. Belibasakis, Porphyromonas gingivalis: an invasive and evasive opportunistic oral pathogen, FEMS Microbiology Letters, vol.5, issue.1, 2012.
DOI : 10.1371/journal.pone.0009321

URL : https://academic.oup.com/femsle/article-pdf/333/1/1/19434944/333-1-1.pdf

Y. R. Brunet, C. S. Bernard, M. Gavioli, R. Lloubès, C. et al., 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

P. I. Eke, B. A. Dye, L. Wei, G. O. Thornton-evans, and R. J. Genco, Prevalence of Periodontitis in Adults in the United States: 2009 and 2010, Journal of Dental Research, vol.91, issue.10, pp.914-934, 2012.
DOI : 10.1111/j.1600-051X.2005.00822.x

R. D. Finn, P. Coggill, R. Y. Eberhardt, S. R. Eddy, J. Mistry et al., The Pfam protein families database: towards a more sustainable future, Nucleic Acids Research, vol.44, issue.D1, pp.279-85, 2016.
DOI : 10.1021/bi9718550

URL : https://hal.archives-ouvertes.fr/hal-01294685

G. Gabarrini, M. De-smit, J. Westra, E. Brouwer, A. Vissink et al., The peptidylarginine deiminase gene is a conserved feature of Porphyromonas gingivalis, Scientific Reports, vol.488, issue.1, 2015.
DOI : 10.1136/annrheumdis-2014-205385

D. G. Gorasia, P. D. Veith, E. G. Hanssen, M. D. Glew, K. Sato et al., Structural Insights into the PorK and PorN Components of the Porphyromonas gingivalis Type IX Secretion System, PLOS Pathogens, vol.25, issue.Suppl 1, 2016.
DOI : 10.1371/journal.ppat.1005820.s011

L. M. Guzman, D. Belin, M. J. Carson, and J. Beckwith, Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter., Journal of Bacteriology, vol.177, issue.14, pp.4121-4151, 1995.
DOI : 10.1128/jb.177.14.4121-4130.1995

URL : http://jb.asm.org/content/177/14/4121.full.pdf

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

M. Hussain, C. M. Stover, and A. Dupont, P. gingivalis in periodontal disease and atherosclerosis -scenes of action for antimicrobial peptides and complement. Front Immunol, 2015.
URL : https://hal.archives-ouvertes.fr/in2p3-01292932

K. M. Janssen, A. Vissink, M. J. De-smit, J. Westra, and E. Brouwer, Lessons to be learned from periodontitis, Current Opinion in Rheumatology, vol.25, issue.2, pp.241-248, 2013.
DOI : 10.1097/BOR.0b013e32835d833d

T. Kadowaki, H. Yukitake, M. Naito, K. Sato, Y. Kikuchi et al., A two-component system regulates gene expression of the type IX secretion component proteins via an ECF sigma factor, Scientific Reports, vol.280, issue.1, 2016.
DOI : 10.1074/jbc.M413544200

J. J. Kamma, M. Nakou, and F. A. Manti, Microbiota of Rapidly Progressive Periodontitis Lesions in Association With Clinical Parameters, Journal of Periodontology, vol.17, issue.11, pp.1073-1081, 1994.
DOI : 10.1177/00220345840630031101

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.5752-5758, 1998.
DOI : 10.1038/ng0797-277

L. A. Kelley, S. Mezulis, C. M. Yates, M. N. Wass, and M. J. Sternberg, The Phyre2 web portal for protein modeling, prediction and analysis, Nature Protocols, vol.1, issue.6, pp.845-58, 2015.
DOI : 10.1093/bioinformatics/btl677

D. Kita, S. Shibata, Y. Kikuchi, E. Kokubu, K. Nakayama et al., ABSTRACT, Applied and Environmental Microbiology, vol.82, issue.6, pp.1756-6603452, 2016.
DOI : 10.1128/AEM.03452-15

J. Koziel, P. Mydel, and J. Potempa, The Link Between Periodontal Disease and Rheumatoid Arthritis: An Updated Review, Current Rheumatology Reports, vol.15, issue.52, 2014.
DOI : 10.1186/ar4376

URL : https://link.springer.com/content/pdf/10.1007%2Fs11926-014-0408-9.pdf

L. Bue, A. M. Nicoletti, G. Toscano, M. A. Rossetti, B. Calì et al., Porphyromonas gingivalis prevalence related to other micro-organisms in adult refractory periodontitis, New Microbiol, vol.22, pp.209-227, 1999.

M. J. Mcbride and D. Nakane, Flavobacterium gliding motility and the type IX secretion system, Current Opinion in Microbiology, vol.28, pp.72-79, 2015.
DOI : 10.1016/j.mib.2015.07.016

M. J. Mcbride and Y. Zhu, Gliding Motility and Por Secretion System Genes Are Widespread among Members of the Phylum Bacteroidetes, Journal of Bacteriology, vol.195, issue.2, pp.270-278, 2013.
DOI : 10.1128/JB.01962-12

K. Nakayama, Porphyromonas gingivalis and related bacteria: from colonial pigmentation to the type IX secretion system and gliding motility, J Periodontal Res, vol.50, 2015.

D. Nakane, K. Sato, H. Wada, M. J. Mcbride, and K. Nakayama, Helical flow of surface protein required for bacterial gliding motility, Proceedings of the National Academy of Sciences, vol.104, issue.49, pp.11145-50, 2013.
DOI : 10.1073/pnas.0704280104

Y. Narita, K. Sato, H. Yukitake, M. Shoji, D. Nakane et al., Lack of a surface layer in Tannerella forsythia mutants deficient in the type IX secretion system, Microbiology, vol.36, issue.4, pp.2295-303, 2014.
DOI : 10.1034/j.1600-0765.2001.036004237.x

K. Paul, J. G. Harmon, and D. F. Blair, Mutational Analysis of the Flagellar Rotor Protein FliN: Identification of Surfaces Important for Flagellar Assembly and Switching, Journal of Bacteriology, vol.188, issue.14, pp.5240-5248, 2006.
DOI : 10.1128/JB.00110-06

S. J. Roman, M. Meyers, K. Volz, and P. Matsumura, A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations., Journal of Bacteriology, vol.174, issue.19, pp.6247-55, 1992.
DOI : 10.1128/jb.174.19.6247-6255.1992

Y. Sagi, S. Khan, and M. Eisenbach, Binding of the Chemotaxis Response Regulator CheY to the Isolated, Intact Switch Complex of the Bacterial Flagellar Motor, Journal of Biological Chemistry, vol.2, issue.28, pp.25867-71, 2003.
DOI : 10.1006/jmbi.2001.4610

M. K. Sarkar, K. Paul, and D. Blair, Chemotaxis signaling protein CheY binds to the rotor protein FliN to control the direction of flagellar rotation in Escherichia coli, Proceedings of the National Academy of Sciences, vol.261, issue.2, pp.9370-9375, 2010.
DOI : 10.1006/jmbi.1996.0453

K. Sato, M. Naito, H. Yukitake, H. Hirakawa, M. Shoji et al., A protein secretion system linked to bacteroidete gliding motility and pathogenesis, Proceedings of the National Academy of Sciences, vol.149, issue.5, pp.276-81, 2010.
DOI : 10.1099/mic.0.25997-0

URL : http://www.pnas.org/content/107/1/276.full.pdf

K. Sato, H. Yukitake, Y. Narita, M. Shoji, M. Naito et al., proteins secreted by the Por secretion system, FEMS Microbiology Letters, vol.23, issue.1, pp.68-76, 2013.
DOI : 10.1111/j.1399-302X.2008.00444.x

URL : https://academic.oup.com/femsle/article-pdf/338/1/68/19125079/338-1-68.pdf

A. Shrivastava and H. C. Berg, Towards a model for Flavobacterium gliding, Current Opinion in Microbiology, vol.28, pp.93-100, 2015.
DOI : 10.1016/j.mib.2015.07.018

URL : http://europepmc.org/articles/pmc4688146?pdf=render

A. Shrivastava, J. J. Johnston, J. M. Van-baaren, and M. J. Mcbride, Flavobacterium johnsoniae GldK, GldL, GldM, and SprA Are Required for Secretion of the Cell Surface Gliding Motility Adhesins SprB and RemA, Journal of Bacteriology, vol.195, issue.14, pp.3201-3213, 1128.
DOI : 10.1128/JB.00333-13

A. Shrivastava, P. P. Lele, and H. C. Berg, A Rotary Motor Drives Flavobacterium Gliding, Current Biology, vol.25, issue.3, 2015.
DOI : 10.1016/j.cub.2014.11.045

URL : https://doi.org/10.1016/j.cub.2014.11.045

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.244-252, 2005.
DOI : 10.1093/nar/gki408

E. L. Sonnhammer, G. Von-heijne, and A. Krogh, A hidden Markov model for predicting transmembrane helices in protein sequences, Proc Int Conf Intell Syst Mol Biol, vol.6, pp.175-82, 1998.

V. Sourjik and N. S. Wingreen, Responding to chemical gradients: bacterial chemotaxis, Current Opinion in Cell Biology, vol.24, issue.2, 2012.
DOI : 10.1016/j.ceb.2011.11.008

URL : http://europepmc.org/articles/pmc3320702?pdf=render

Y. Taguchi, K. Sato, H. Yukitake, T. Inoue, M. Nakayama et al., Involvement of an Skp-Like Protein, PGN_0300, in the Type IX Secretion System of Porphyromonas gingivalis, Infection and Immunity, vol.84, issue.1, pp.230-270, 1128.
DOI : 10.1128/IAI.01308-15

M. B. Tomek, L. Neumann, I. Nimeth, A. Koerdt, P. Andesner et al., -glycosylation, Molecular Oral Microbiology, vol.298, issue.Suppl. 1, pp.307-327, 2014.
DOI : 10.1126/science.298.5599.1790

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

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

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.623-631, 2006.
DOI : 10.1038/nmeth895

Y. Zhu and M. J. Mcbride, Deletion of the Cytophaga hutchinsonii type IX secretion system gene sprP results in defects in gliding motility and cellulose utilization, Applied Microbiology and Biotechnology, vol.97, issue.9, pp.763-75, 2014.
DOI : 10.1007/s00253-012-4259-x

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.27031-27072, 2013.
DOI : 10.1371/journal.pone.0067647

URL : https://hal.archives-ouvertes.fr/hal-01458230

. Unbound, and bound proteins were collected and analyzed by SDS- PAGE and Coomassie blue staining. The different proteins are indicated on the right. Molecular weight markers (in kDa) are indicated on the left

. Coli-heterologous-host, Relative fluorescence levels (in arbitrary units) of E. coli cells carrying the indicated pUA66-promoter derivatives (GFP under the control of the indicated promoter) in absence (-, white bars) or presence (+, blue bars) or PorX. Is represented the mean of fluorescence levels obtained from three independent experiments (each measured in triplicate) The production of VSV-G-tagged PorX is shown on bottom (immunodetection with anti-VSV-G monoclonal antibody