S. S. Abby, J. Cury, J. Guglielmini, B. Neron, M. Touchon et al., Identification of protein secretion systems in bacterial genomes, Sci. Rep, vol.6, p.23080, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01677379

C. J. Alteri, S. D. Himpsl, S. R. Pickens, J. R. Lindner, J. S. Zora et al., Multicellular bacteria deploy the Type VI secretion system to preemptively strike neighboring cells, PLoS Path, vol.9, p.1003608, 2013.
DOI : 10.1371/journal.ppat.1003608
URL : https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1003608&type=printable

K. A. Aly, E. T. Beebe, C. H. Chan, M. A. Goren, C. Sepulveda et al., Cell-free production of integral membrane aspartic acid proteases reveals zinc-dependent methyltransferase activity of the Pseudomonas aeruginosa prepilin peptidase PilD, vol.2, pp.94-104, 2013.

Y. An, J. Wang, C. Li, A. Leier, T. Marquez-lago et al., Comprehensive assessment and performance improvement of effector protein predictors for bacterial secretion systems III, IV and VI, 2016.
DOI : 10.1093/bib/bbw100

L. S. Ates, E. N. Houben, and W. Bitter, Type VII secretion: a highly versatile secretion system, 2016.
DOI : 10.1128/microbiolspec.vmbf-0011-2015

G. Ball, H. Antelmann, P. R. Imbert, M. R. Gimenez, R. Voulhoux et al., Contribution of the Twin Arginine Translocation system to the exoproteome of Pseudomonas aeruginosa, Sci. Rep, vol.6, p.27675, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01458178

M. Basler, Type VI secretion system: secretion by a contractile nanomachine, Philos. Trans. R. Soc. Lond. B. Biol. Sci, vol.370, 2015.
DOI : 10.1098/rstb.2015.0021
URL : http://rstb.royalsocietypublishing.org/content/370/1679/20150021.full.pdf

H. Bedouelle, P. J. Bassford, A. V. Fowler, I. Zabin, J. Beckwith et al., Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli, Nature, vol.285, pp.78-81, 1980.

B. C. Berks, The twin-arginine protein translocation pathway, Annu. Rev. Biochem, vol.84, pp.843-864, 2015.
DOI : 10.1146/annurev-biochem-060614-034251

H. D. Bernstein, Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway, Mol. Microbiol, vol.97, pp.205-215, 2015.

J. L. Berry, P. , and V. , Exceptionally widespread nanomachines composed of type IV pilins: the prokaryotic Swiss Army knives, FEMS Microbiol. Rev, vol.39, pp.134-154, 2015.

R. N. Besingi, C. , and P. L. , Extracellular protease digestion to evaluate membrane protein cell surface localization, Nat. Protoc, vol.10, pp.2074-2080, 2015.
DOI : 10.1038/nprot.2015.131
URL : http://europepmc.org/articles/pmc4838181?pdf=render

G. Briones, D. Hofreuter, and J. E. Galan, Cre reporter system to monitor the translocation of type III secreted proteins into host cells, Infect. Immun, vol.74, pp.1084-1090, 2006.

Y. R. Brunet, L. Espinosa, S. Harchouni, T. Mignot, C. et al., Imaging type VI secretion-mediated bacterial killing, Cell Rep, vol.3, pp.36-41, 2013.
DOI : 10.1016/j.celrep.2012.11.027
URL : https://hal.archives-ouvertes.fr/hal-01458227

F. X. Campbell-valois, P. Schnupf, G. Nigro, M. Sachse, P. J. Sansonetti et al., A Fluorescent Reporter Reveals On/Off Regulation of the Shigella Type III Secretion Apparatus during Entry and Cell-to-Cell Spread, Cell Host Microbe, vol.15, pp.177-189, 2014.

E. M. Campodonico, L. Chesnel, R. , and C. R. , A yeast genetic system for the identification and characterization of substrate proteins transferred into host cells by the Legionella pneumophila Dot/Icm system, Mol. Microbiol, vol.56, pp.918-933, 2005.

Z. Cao, M. G. Casabona, H. Kneuper, J. D. Chalmers, P. et al., The type VII secretion system of Staphylococcus aureus secretes a nuclease toxin that targets competitor bacteria, Nat. Microbiol, vol.2, pp.1-11, 2016.

K. L. Carey, H. J. Newton, A. Lührmann, R. , and C. R. , The Coxiella burnetii Dot/Icm System Delivers a Unique Repertoire of Type IV Effectors into Host Cells and Is Required for Intracellular Replication, PLoS Path, vol.7, p.1002056, 2011.

Y. W. Chang, L. A. Rettberg, A. Treuner-lange, J. Iwasa, L. Sogaard-andersen et al., Architecture of the type IVa pilus machine, Science, vol.351, p.2001, 2016.

X. Charpentier, O. , and E. , Identification of the secretion and translocation domain of the enteropathogenic and enterohemorrhagic Escherichia coli effector Cif, using TEM-1 beta-lactamase as a new fluorescence-based reporter, J. Bacteriol, vol.186, pp.5486-5495, 2004.

Y. S. Chen, R. J. Bastidas, H. A. Saka, V. K. Carpenter, K. L. Richards et al., The Chlamydia trachomatis type III secretion chaperone Slc1 engages multiple early effectors, including TepP, a tyrosine-phosphorylated protein required for the recruitment of CrkI-II to nascent inclusions and innate immune signaling, PLoS Pathog, vol.10, p.1003954, 2014.

J. Y. Choi, T. H. Jang, and H. H. Park, The mechanism of folding robustness revealed by the crystal structure of extra-superfolder GFP, FEBS Lett, vol.591, pp.442-447, 2017.

P. J. Christie, N. Whitaker, and C. Gonzalez-rivera, Mechanism and structure of the bacterial type IV secretion systems, Biochim. Biophys. Acta, vol.1843, pp.1578-1591, 2014.

T. R. Costa, C. Felisberto-rodrigues, A. Meir, M. S. Prevost, A. Redzej et al., Secretion systems in Gram-negative bacteria: structural and mechanistic insights, Nat. Rev. Microbiol, vol.13, pp.343-359, 2015.

C. E. Cowles, Y. Li, M. F. Semmelhack, I. M. Cristea, and T. J. Silhavy, The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli, Mol. Microbiol, vol.79, pp.1168-1181, 2011.

J. B. Day, F. Ferracci, G. V. Plano, I. De-diego, M. Ksiazek et al., Translocation of YopE and YopN into eukaryotic cells by Yersinia pestis yopN, tyeA, sycN, yscB and lcrG deletion mutants measured using a phosphorylatable peptide tag and phosphospecific antibodies, Mol. Microbiol, vol.47, p.23123, 2003.

C. Enfert, C. Chapon, and A. P. Pugsley, Export and secretion of the lipoprotein pullulanase by Klebsiella pneumoniae, Mol. Microbiol, vol.1, pp.107-116, 1987.

M. Desvaux, M. Hebraud, R. Talon, H. , and I. R. , Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue, Trends Microbiol, vol.17, pp.139-145, 2009.

K. Dohlich, A. B. Zumsteg, C. Goosmann, and M. Kolbe, A substratefusion protein is trapped inside the Type III secretion system channel in Shigella flexneri, PLoS Path, vol.10, p.1003881, 2014.

F. Duong and W. Wickner, Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme, EMBO J, vol.16, pp.2756-2768, 1997.

A. East, A. E. Mechaly, G. H. Huysmans, C. Bernarde, D. Tello-manigne et al., Structural basis of pullulanase membrane binding and secretion revealed by X-Ray crystallography, molecular dynamics and biochemical analysis, Structure, vol.24, pp.92-104, 2016.
URL : https://hal.archives-ouvertes.fr/pasteur-01498343

S. Ehsani, C. D. Rodrigues, and J. Enninga, Turning on the spotlight-using light to monitor and characterize bacterial effector secretion and translocation, Curr. Opin. Microbiol, vol.12, pp.24-30, 2009.
URL : https://hal.archives-ouvertes.fr/pasteur-01899508

J. Enninga, J. Mounier, P. Sansonetti, and G. Tran-van-nhieu, Secretion of type III effectors into host cells in real time, Nat. Methods, vol.2, pp.959-965, 2005.

B. J. Feilmeier, G. Iseminger, D. Schroeder, H. Webber, and G. J. Phillips, Green fluorescent protein functions as a reporter for protein localization in Escherichia coli, J. Bacteriol, vol.182, pp.4068-4076, 2000.

O. Francetic, N. Buddelmeijer, S. Lewenza, C. A. Kumamoto, and A. P. Pugsley, Signal recognition particle-dependent inner membrane targeting of the PulG Pseudopilin component of a type II secretion system, J. Bacteriol, vol.189, pp.1783-1793, 2007.
URL : https://hal.archives-ouvertes.fr/hal-00138935

O. Francetic, M. P. Hanson, and C. A. Kumamoto, prlA suppression of defective export of maltose-binding protein in secB mutants of Escherichia coli, J. Bacteriol, vol.175, pp.4036-4044, 1993.

O. Francetic and A. P. Pugsley, Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca, J. Bacteriol, vol.187, pp.7045-7055, 2005.

M. B. Frankel, B. M. Wojcik, A. C. Dedent, D. M. Missiakas, and O. Schneewind, ABI domain-containing proteins contribute to surface protein display and cell division in Staphylococcus aureus, Mol. Microbiol, vol.78, pp.238-252, 2010.

D. Gagic, M. Ciric, W. X. Wen, F. Ng, R. et al., Exploring the secretomes of microbes and microbial communities using filamentous phage display, Front. Microbiol, vol.7, p.429, 2016.

J. T. Garcia, F. Ferracci, M. W. Jackson, S. S. Joseph, I. Pattis et al., Measurement of effector protein injection by type III and type IV secretion systems by using a 13-residue phosphorylatable glycogen synthase kinase tag, Infect. Immun, vol.74, pp.5645-5657, 2006.

J. A. Gawthorne, L. Audry, C. Mcquitty, P. Dean, J. M. Christie et al., Visualizing the translocation and localization of bacterial Type III effector proteins by using a genetically encoded reporter system, Appl. Environ. Microbiol, vol.82, pp.2700-2708, 2016.
URL : https://hal.archives-ouvertes.fr/pasteur-01899443

I. Gelis, A. M. Bonvin, D. Keramisanou, M. Koukaki, G. Gouridis et al., Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR, Cell, vol.131, pp.756-769, 2007.

E. R. Green and J. Mecsas, Bacterial secretion systems: an overview, 2016.

C. R. Guan, W. J. Cui, J. T. Cheng, R. Liu, Z. M. Liu et al., Construction of a highly active secretory expression system via an engineered dual promoter and a highly efficient signal peptide in Bacillus subtilis, N. Biotechnol, vol.33, pp.372-379, 2016.

I. Guilvout, M. Chami, C. Berrier, A. Ghazi, A. Engel et al., in vitro multimerization and membrane insertion of bacterial outer membrane secretin PulD, J. Mol. Biol, vol.382, pp.13-23, 2008.

T. Hara, S. Matsuyama, and H. Tokuda, Mechanism underlying the inner membrane retention of Escherichia coli lipoproteins caused by Lol avoidance signals, J. Biol. Chem, vol.278, pp.40408-40414, 2003.

T. M. Heggeset, V. Kucharova, I. Naerdal, S. Valla, H. Sletta et al., Combinatorial mutagenesis and selection of improved signal sequences and their application for high-level production of translocated heterologous proteins in Escherichia coli, Appl. Environ. Microbiol, vol.79, pp.559-568, 2013.

M. Heidtman, E. J. Chen, M. Y. Moy, and R. R. Isberg, Largescale identification of Legionella pneumophila Dot/Icm substrates that modulate host cell vesicle trafficking pathways, Cell. Microbiol, vol.11, pp.230-248, 2009.

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, pp.9-21, 2014.

R. D. Hood, P. Singh, F. Hsu, T. Guvener, M. A. Carl et al., A type VI secretion system of Pseudomonas aeruginosa targets a toxin to bacteria, Cell Host Microbe, vol.7, pp.25-37, 2010.

G. Hortensia-rolán, E. Durand, A. Mecsas, and J. , Identifying Yersinia YopH-Targeted signal transduction pathways that impair neutrophil responses during in vivo murine infection, Cell Host Microbe, vol.14, pp.306-317, 2013.

H. A. Howell, L. K. Logan, and A. R. Hauser, Type III secretion of ExoU is critical during early Pseudomonas aeruginosa pneumonia, vol.4, pp.32-45, 2013.

B. Hu, M. Lara-tejero, Q. Kong, J. E. Galán, and J. Liu, In situ molecular architecture of the salmonella Type III secretion machine, Cell, vol.168, pp.1065-1074, 2017.

D. Huber, D. Boyd, Y. Xia, M. H. Olma, M. Gerstein et al., Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation, J. Bacteriol, vol.187, pp.2983-2991, 2005.

R. Ieva, P. Tian, J. H. Peterson, and H. D. Bernstein, Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain, Proc. Natl. Acad. Sci. U.S.A, vol.108, 2011.

K. Ito, M. Wittekind, M. Nomura, K. Shiba, T. Yura et al., A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteins, Cell, vol.32, pp.789-797, 1983.

S. Jackowski, R. , and C. O. , Transfer of fatty acids from the 1-position of phosphatidylethanolamine to the major outer membrane lipoprotein of Escherichia coli, J. Biol. Chem, vol.261, pp.11328-11333, 1986.

R. C. Jackson and G. Blobel, Post-translational cleavage of presecretory proteins with an extract of rough microsomes from dog pancreas containing signal peptidase activity, Proc. Natl. Acad. Sci. U.S.A, vol.74, pp.5598-5602, 1977.

K. Jacobsson and L. Frykberg, Phage display shot-gun cloning of ligandbinding domains of prokaryotic receptors approaches 100% correct clones, Biotechniques, vol.20, pp.1080-1081, 1996.

V. Jaumouille, O. Francetic, P. J. Sansonetti, T. Van-nhieu, and G. , Cytoplasmic targeting of IpaC to the bacterial pole directs polar type III secretion in Shigella, EMBO J, vol.27, pp.447-457, 2008.

A. S. Juncker, H. Willenbrock, G. Von-heijne, S. Brunak, H. Nielsen et al., Prediction of lipoprotein signal peptides in Gram-negative bacteria, Protein Sci, vol.12, pp.1652-1662, 2003.

K. Kanonenberg, C. K. Schwarz, and L. Schmitt, Type I secretion systems-a story of appendices, Res. Microbiol, vol.164, pp.596-604, 2013.

G. Karimova, J. Pidoux, A. Ullmann, and D. Ladant, A bacterial twohybrid system based on a reconstituted signal transduction pathway, Proc. Natl. Acad. Sci. U.S.A, vol.95, pp.5752-5756, 1998.

B. Kenny and B. B. Finlay, Protein secretion by enteropathogenic Escherichia coli is essential for transducing signals to epithelial cells, Proc. Natl. Acad. Sci. U.S.A, vol.92, pp.7991-7995, 1995.

T. J. Kirn, N. Bose, T. , and R. K. , Secretion of a soluble colonization factor by the TCP type 4 pilus biogenesis pathway in Vibrio cholerae, Mol. Microbiol, vol.49, pp.81-92, 2003.

A. Konovalova, D. H. Perlman, C. E. Cowles, and T. J. Silhavy, Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of beta-barrel proteins, Proc. Natl. Acad. Sci. U.S.A, vol.111, 2014.

K. V. Korotkov, M. Sandkvist, and W. G. Hol, The type II secretion system: biogenesis, molecular architecture and mechanism, Nat. Rev. Microbiol, vol.10, pp.336-351, 2012.

P. Kreutzenbeck, C. Kroger, F. Lausberg, N. Blaudeck, G. A. Sprenger et al., Escherichia coli twin arginine (Tat) mutant translocases possessing relaxed signal peptide recognition specificities, J. Biol. Chem, vol.282, pp.7903-7911, 2007.

C. A. Kumamoto and P. M. Gannon, Effects of Escherichia coli secB mutations on pre-maltose binding protein conformation and export kinetics, J. Biol. Chem, vol.263, pp.11554-11558, 1988.

O. S. Kumru, R. J. Schulze, J. G. Slusser, and W. R. Zuckert, Development and validation of a FACS-based lipoprotein localization screen in the Lyme disease spirochete Borrelia burgdorferi, BMC Microbiol, vol.10, p.277, 2010.

F. Lausberg, S. Fleckenstein, P. Kreutzenbeck, J. Frobel, P. Rose et al., Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli, PLoS ONE, vol.7, p.39867, 2012.

S. Lewenza, D. Vidal-ingigliardi, and A. P. Pugsley, Direct visualization of red fluorescent lipoproteins indicates conservation of the membrane sorting rules in the family Enterobacteriaceae, J. Bacteriol, vol.188, pp.3516-3524, 2006.

D. L. Leyton, A. E. Rossiter, H. , and I. R. , From self sufficiency to dependence: mechanisms and factors important for autotransporter biogenesis, Nat. Rev. Microbiol, vol.10, pp.213-225, 2012.

L. Li, E. Park, J. Ling, J. Ingram, H. Ploegh et al., Crystal structure of a substrate-engaged SecY protein-translocation channel, Nature, vol.531, pp.395-399, 2016.

J. Lin, Y. Zou, C. Ma, Q. She, Y. Liang et al., Heterologous expression of mannanase and developing a new reporter gene system in Lactobacillus casei and Escherichia coli, PLoS ONE, vol.10, 2015.

L. Logger, M. S. Aschtgen, M. Guerin, E. Cascales, D. et al., Molecular dissection of the interface between the Type VI secretion TssM cytoplasmic domain and the TssG baseplate component, J. Mol. Biol, vol.428, pp.4424-4437, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01780174

F. Lonjon, M. Turner, C. Henry, D. Rengel, D. Lohou et al., Comparative secretome analysis of Ralstonia solanacearum Type 3 secretion-associated mutants reveals a fine control of effector delivery, essential for bacterial pathogenicity, Mol. Cell. Proteomics, vol.15, pp.598-613, 2016.

Z. Q. Luo and R. R. Isberg, Multiple substrates of the Legionella pneumophila Dot/Icm system identified by interbacterial protein transfer, Proc. Natl. Acad. Sci. U.S.A, vol.101, pp.841-846, 2004.

S. R. Lybarger, T. L. Johnson, M. D. Gray, A. E. Sikora, and M. Sandkvist, Docking and assembly of the type II secretion complex of Vibrio cholerae, J. Bacteriol, vol.191, pp.3149-3161, 2009.

J. A. Lycklama-a-nijeholt and A. J. Driessen, The bacterial Sec-translocase: structure and mechanism, Philos. Trans. R. Soc. Lond. B. Biol. Sci, vol.367, pp.1016-1028, 2012.

A. Mahdavi, J. Szychowski, J. T. Ngo, M. J. Sweredoski, R. L. Graham et al., Identification of secreted bacterial proteins by noncanonical amino acid tagging, Proc. Natl. Acad. Sci. U.S.A, vol.111, pp.433-438, 2014.
DOI : 10.1073/pnas.1301740111
URL : http://www.pnas.org/content/111/1/433.full.pdf

C. Manoil and J. Beckwith, TnphoA: a transposon probe for protein export signals, Proc. Natl. Acad. Sci. U.S.A, vol.82, pp.8129-8133, 1985.
DOI : 10.1073/pnas.82.23.8129
URL : http://www.pnas.org/content/82/23/8129.full.pdf

A. W. Maresso, R. Wu, J. W. Kern, R. Zhang, D. Janik et al., Activation of inhibitors by sortase triggers irreversible modification of the active site, J. Biol. Chem, vol.282, pp.23129-23139, 2007.

G. Mathiesen, A. Sveen, M. B. Brurberg, L. Fredriksen, L. Axelsson et al., Genome-wide analysis of signal peptide functionality in Lactobacillus plantarum WCFS1, BMC Genomics, vol.10, p.425, 2009.

M. Mavris, A. L. Page, R. Tournebize, B. Demers, P. Sansonetti et al., Regulation of transcription by the activity of the Shigella flexneri type III secretion apparatus, Mol. Microbiol, vol.43, pp.1543-1553, 2002.

D. F. Meyer, C. Noroy, A. Moumene, S. Raffaele, E. Albina et al., Searching algorithm for type IV secretion system effectors 1.0: a tool for predicting type IV effectors and exploring their genomic context, Nucleic Acids Res, vol.41, pp.9218-9229, 2013.

E. Mills, K. Baruch, G. Aviv, M. Nitzan, R. et al., Dynamics of the Type III secretion system activity of enteropathogenic Escherichia coli, vol.4, pp.303-316, 2013.

D. T. Moir, M. Di, E. Wong, R. A. Moore, H. P. Schweizer et al., Development and application of a cellular, gain-ofsignal, bioluminescent reporter screen for inhibitors of Type II secretion in Pseudomonas aeruginosa and Burkholderia pseudomallei, J. Biomol. Screen, vol.16, pp.694-705, 2011.

M. P. Molloy, B. R. Herbert, M. B. Slade, T. Rabilloud, A. S. Nouwens et al., Proteomic analysis of the Escherichia coli outer membrane, Eur. J. Biochem, vol.267, pp.2871-2881, 2000.

F. Monteiro, S. Genin, I. Van-dijk, and M. Valls, A luminescent reporter evidences active expression of Ralstonia solanacearum type III secretion system genes throughout plant infection, Microbiol. Sgm, vol.158, pp.2107-2116, 2012.

K. E. Mueller and K. A. Fields, Application of ?-lactamase reporter fusions as an indicator of effector protein secretion during infections with the obligate intracellular pathogen Chlamydia trachomatis, PLoS ONE, vol.10, 2015.

M. Nivaskumar, J. Santos-moreno, C. Malosse, N. Nadeau, J. Chamot-rooke et al., Pseudopilin residue E5 is essential for recruitment by the type 2 secretion system assembly platform, Mol. Microbiol, vol.101, pp.924-941, 2016.
DOI : 10.1111/mmi.13432
URL : https://onlinelibrary.wiley.com/doi/pdf/10.1111/mmi.13432

J. Pallier, W. Aucher, M. Pires, and N. Buddelmeijer, Phosphatidyllycerol::prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments and its essential residues are embedded in the membrane, J. Bacteriol, vol.194, pp.2142-2151, 2012.

T. Palmer and B. C. Berks, The twin-arginine translocation (Tat) protein export pathway, Nat. Rev. Microbiol, vol.10, pp.483-496, 2012.
DOI : 10.1038/nrmicro2814

S. H. Payne, S. Bonissone, S. Wu, R. N. Brown, D. N. Ivankov et al., Unexpected diversity of signal peptides in prokaryotes, vol.3, pp.339-351, 2012.

E. F. Perkowski, K. E. Zulauf, D. Weerakoon, J. D. Hayden, T. R. Ioerger et al., The EXIT strategy: an approach for identifying bacterial proteins exported during host infection, vol.8, pp.333-350, 2017.
DOI : 10.1128/mbio.00333-17
URL : https://mbio.asm.org/content/mbio/8/2/e00333-17.full.pdf

T. N. Petersen, S. Brunak, G. Von-heijne, and H. Nielsen, SignalP 4.0: discriminating signal peptides from transmembrane regions, Nat. Methods, vol.8, pp.785-786, 2011.

C. Pineau, N. Guschinskaya, X. Robert, P. Gouet, L. Ballut et al., Substrate recognition by the bacterial type II secretion system: more than a simple interaction, Mol. Microbiol, vol.94, pp.126-140, 2014.
DOI : 10.1111/mmi.12744
URL : https://hal.archives-ouvertes.fr/hal-02001308

O. M. Possot, L. Letellier, and A. P. Pugsley, Energy requirement for pullulanase secretion by the main terminal branch of the general secretory pathway, Mol. Microbiol, vol.24, pp.457-464, 1997.

H. Remaut, C. Tang, N. S. Henderson, J. S. Pinkner, T. Wang et al., Fiber formation across the bacterial outer membrane by the chaperone/usher pathway, Cell, vol.133, pp.640-652, 2008.
DOI : 10.1016/j.cell.2008.03.033
URL : https://doi.org/10.1016/j.cell.2008.03.033

K. E. Riordan, J. A. Sorg, B. J. Berube, and O. Schneewind, Impassable YscP substrates and their impact on the Yersinia enterocolitica type III secretion pathway, J. Bacteriol, vol.190, pp.6204-6216, 2008.
DOI : 10.1128/jb.00467-08
URL : https://jb.asm.org/content/190/18/6204.full.pdf

A. Rondelet, C. , and G. , Type II secretion: the substrates that won't go away, Res. Microbiol, vol.164, pp.556-561, 2013.
DOI : 10.1016/j.resmic.2013.03.005
URL : https://hal.archives-ouvertes.fr/hal-02001302

H. A. Saka, J. W. Thompson, Y. S. Chen, L. G. Dubois, J. T. Haas et al., Chlamydia trachomatis infection leads to defined alterations to the lipid droplet proteome in epithelial cells, PLoS ONE, vol.10, p.124630, 2015.

K. Sato, M. Naito, H. Yukitake, H. Hirakawa, M. Shoji et al., A protein secretion system linked to bacteroidete gliding motility and pathogenesis, Proc. Natl. Acad. Sci. U.S.A, vol.107, pp.276-281, 2010.
DOI : 10.1073/pnas.0912010107
URL : http://www.pnas.org/content/107/1/276.full.pdf

N. Sauvonnet and A. P. Pugsley, Identification of two regions of Klebsiella oxytoca pullulanase that together are capable of promoting betalactamase secretion by the general secretory pathway, Mol. Microbiol, vol.22, pp.1-7, 1996.

M. C. Schlumberger, A. J. Muller, K. Ehrbar, B. Winnen, I. Duss et al., Real-time imaging of type III secretion: Salmonella SipA injection into host cells, Proc. Natl. Acad. Sci. U.S.A, vol.102, pp.12548-12553, 2005.

O. Schneewind and D. Missiakas, Sec-secretion and sortase-mediated anchoring of proteins in Gram-positive bacteria, Biochim. Biophys. Acta, vol.1843, pp.1687-1697, 2014.

A. Seydel, P. Gounon, and A. P. Pugsley, Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection, Mol. Microbiol, vol.34, pp.810-821, 1999.

N. C. Shaner, R. E. Campbell, P. A. Steinbach, B. N. Giepmans, A. E. Palmer et al., Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein, Nat. Biotechnol, vol.22, pp.1567-1572, 2004.
DOI : 10.1038/nbt1037

H. A. Shuman and T. J. Silhavy, The art and design of genetic screens: Escherichia coli, Nat. Rev. Genet, vol.4, pp.419-431, 2003.

J. M. Silverman, D. M. Agnello, H. Zheng, B. T. Andrews, M. Li et al., Haemolysin coregulated protein is an exported receptor and chaperone of type VI secretion substrates, Mol. Cell, vol.51, pp.584-593, 2013.
DOI : 10.1016/j.molcel.2013.07.025
URL : https://doi.org/10.1016/j.molcel.2013.07.025

S. H. Sinclair, J. C. Garcia-garcia, and J. S. Dumler, Bioinformatic and mass spectrometry identification of Anaplasma phagocytophilum proteins translocated into host cell nuclei, Front. Microbiol, vol.6, p.55, 2015.
DOI : 10.3389/fmicb.2015.00055
URL : https://www.frontiersin.org/articles/10.3389/fmicb.2015.00055/pdf

J. L. Sisko, K. Spaeth, Y. Kumar, and R. H. Valdivia, Multifunctional analysis of Chlamydia-specific genes in a yeast expression system, Mol. Microbiol, vol.60, pp.51-66, 2006.

N. L. Slagowski, R. W. Kramer, M. F. Morrison, J. Labaer, and C. F. Lesser, A functional genomic yeast screen to identify pathogenic bacterial proteins, PLoS Pathog, vol.4, p.9, 2008.
DOI : 10.1371/journal.ppat.0040009
URL : https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.0040009&type=printable

M. P. Sory, C. , and G. R. , Translocation of a hybrid YopEadenylate cyclase from Yersinia enterocolitica into HeLa cells, Mol. Microbiol, vol.14, pp.583-594, 1994.

A. Subtil, C. Delevoye, M. E. Bala, L. Tastevin, S. Perrinet et al., A directed screen for chlamydial proteins secreted by a type III mechanism identifies a translocated protein and numerous other new candidates, Mol. Microbiol, vol.56, pp.1636-1647, 2005.
URL : https://hal.archives-ouvertes.fr/hal-00021366

A. Subtil, C. Parsot, and A. Varsat, Secretion of predicted Inc proteins of Chlamydia pneumoniae by a heterologous type III machinery, Mol. Microbiol, vol.39, pp.792-800, 2001.

J. D. Thomas, R. A. Daniel, J. Errington, R. , and C. , Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli, Mol. Microbiol, vol.39, pp.47-53, 2001.

M. L. Urbanowski, G. L. Lykken, Y. , and T. L. , A secreted regulatory protein couples transcription to the secretory activity of the Pseudomonas aeruginosa type III secretion system, Proc. Natl. Acad. Sci. U.S.A, vol.102, pp.9930-9935, 2005.

S. B. Van-engelenburg, P. , and A. E. , Quantification of real-time Salmonella effector type III secretion kinetics reveals differential secretion rates for SopE2 and SptP, Chem. Biol, vol.15, pp.619-628, 2008.

S. B. Van-engelenburg, P. , and A. E. , Imaging type-III secretion reveals dynamics and spatial segregation of Salmonella effectors, Nat. Methods, vol.7, pp.325-330, 2010.

N. Van-gerven, R. D. Klein, S. J. Hultgren, R. , and H. , Bacterial amyloid formation: structural insights into curli biogensis, Trends Microbiol, vol.23, pp.693-706, 2015.

G. Von-heijne, The signal peptide, J. Membr. Biol, vol.115, pp.195-201, 1990.

R. Voulhoux, M. P. Bos, J. Geurtsen, M. Mols, and J. Tommassen, Role of a highly conserved bacterial protein in outer membrane protein assembly, Science, vol.299, pp.262-265, 2003.

G. Q. Wang, Y. J. Xia, Z. Q. Xiong, H. Zhang, A. et al., Use of a novel report protein to study the secretion signal of Flagellin in Bacillus subtilis, Curr. Microbiol, vol.73, pp.242-247, 2016.

T. Wille, K. Blank, C. Schmidt, V. Vogt, and R. G. Gerlach, Gaussia princeps luciferase as a reporter for transcriptional activity, protein secretion, and protein-protein interactions in Salmonella enterica Serovar Typhimurium, Appl. Environ. Microbiol, vol.78, pp.250-257, 2012.

M. M. Wilson, D. E. Anderson, and H. D. Bernstein, Analysis of the outer membrane proteome and secretome of Bacteroides fragilis reveals a multiplicity of secretion mechanisms, PLoS ONE, vol.10, 2015.

M. M. Wilson and H. D. Bernstein, Surface-Exposed Lipoproteins: an emerging secretion phenomenon in gram-negative bacteria, Trends Microbiol, vol.24, pp.198-208, 2016.

T. Wu, J. Malinverni, N. Ruiz, S. Kim, T. J. Silhavy et al., Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli, Cell, vol.121, pp.235-245, 2005.

J. S. Yount, L. K. Tsou, P. D. Dossa, A. L. Kullas, A. W. Van-der-velden et al., Visible fluorescence detection of type III protein secretion from bacterial pathogens, J. Am. Chem. Soc, vol.132, pp.8244-8245, 2010.

W. Zhu, S. Banga, Y. Tan, C. Zheng, R. Stephenson et al., Comprehensive identification of protein substrates of the Dot/Icm Type IV Transporter of Legionella pneumophila, PLoS ONE, vol.6, 2011.

W. Zückert, Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond, Biochem. Biophys. Acta Mol. Cell Res, vol.1843, pp.1509-1516, 2014.

M. Zuverink and J. T. Barbieri, From GFP to ?-lactamase: advancing intact cell imaging for toxins and effectors, Pathog. Dis, vol.73, p.97, 2015.