Detailed information of component protein


Summary

Component ID T6CP259499
Component protein type TssI
T6SS ID (Type) T6SS00003 experimental (Type i3)
Strain Pseudomonas aeruginosa PAO1
Replicon chromosome (H1-T6SS)
Sequence Protein sequence (1020 a.a.); Nucleotide sequence (3060 bp)
Reference
[1] LeRoux M, De Leon JA, Kuwada NJ, et al. Quantitative single-cell characterization of bacterial interactions reveals type VI secretion is a double-edged sword. Proc Natl Acad Sci U S A. 2012 Nov 27;109(48):19804-9. doi: 10.1073/pnas.1213963109. Epub 2012 Nov 12. PMID: 23150540
[2] Lossi NS, Manoli E, Simpson P, et al. The archetype Pseudomonas aeruginosa proteins TssB and TagJ form a novel subcomplex in the bacterial type VI secretion system. Mol Microbiol. 2012 Oct;86(2):437-56. doi: 10.1111/j.1365-2958.2012.08204.x. Epub 2012 Aug 29. PMID: 22906320
[3] Chou S, Bui NK, Russell AB, et al. Structure of a peptidoglycan amidase effector targeted to Gram-negative bacteria by the type VI secretion system. Cell Rep. 2012 Jun 28;1(6):656-64. doi: 10.1016/j.celrep.2012.05.016. Epub 2012 May 31. PMID: 22813741
[4] Casabona MG, Silverman JM, Sall KM, et al. An ABC transporter and an outer membrane lipoprotein participate in posttranslational activation of type VI secretion in Pseudomonas aeruginosa. Environ Microbiol. 2013 Feb;15(2):471-86. doi: 10.1111/j.1462-2920.2012.02816.x. Epub 2012 Jul 6. PMID: 22765374
[5] Zhang H, Gao ZQ, Su XD, et al. Crystal structure of type VI effector Tse1 from Pseudomonas aeruginosa. FEBS Lett. 2012 Sep 21;586(19):3193-9. doi: 10.1016/j.febslet.2012.06.036. Epub 2012 Jun 29. PMID: 22750141
[6] Ding J, Wang W, Feng H, et al. Structural insights into the Pseudomonas aeruginosa type VI virulence effector Tse1 bacteriolysis and self-protection mechanisms. J Biol Chem. 2012 Aug 3;287(32):26911-20. doi: 10.1074/jbc.M112.368043. Epub 2012 Jun 14. PMID: 22700987
[7] Kefala K, Kotsifaki D, Providaki M, et al. Purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal fragment of the MvfR protein from Pseudomonas aeruginosa. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):695-7. doi: 10.1107/S1744309112016661. Epub 2012 May 23. PMID: 22684073
[8] Sana TG, Hachani A, Bucior I, et al. The second type VI secretion system of Pseudomonas aeruginosa strain PAO1 is regulated by quorum sensing and Fur and modulates internalization in epithelial cells. J Biol Chem. 2012 Aug 3;287(32):27095-105. doi: 10.1074/jbc.M112.376368. Epub 2012 Jun 4. PMID: 22665491
[9] Li M, Le Trong I, Carl MA, et al. Structural basis for type VI secretion effector recognition by a cognate immunity protein. PLoS Pathog. 2012;8(4):e1002613. doi: 10.1371/journal.ppat.1002613. Epub 2012 Apr 12. PMID: 22511866
[10] Zou T, Yao X, Qin B, et al. Crystal structure of Pseudomonas aeruginosa Tsi2 reveals a stably folded superhelical antitoxin. J Mol Biol. 2012 Apr 6;417(4):351-61. doi: 10.1016/j.jmb.2012.01.040. Epub 2012 Jan 30. PMID: 22310046
[11] Silverman JM, Austin LS, Hsu F, et al. Separate inputs modulate phosphorylation-dependent and -independent type VI secretion activation. Mol Microbiol. 2011 Dec;82(5):1277-90. doi: 10.1111/j.1365-2958.2011.07889.x. Epub 2011 Nov 4. PMID: 22017253
[12] Goldová J, Ulrych A, Hercík K, et al. A eukaryotic-type signalling system of Pseudomonas aeruginosa contributes to oxidative stress resistance, intracellular survival and virulence. BMC Genomics. 2011 Aug 31;12:437. doi: 10.1186/1471-2164-12-437. PMID: 21880152
[13] Lossi NS, Dajani R, Freemont P, et al. Structure-function analysis of HsiF, a gp25-like component of the type VI secretion system, in Pseudomonas aeruginosa. Microbiology (Reading). 2011 Dec;157(Pt 12):3292-3305. doi: 10.1099/mic.0.051987-0. Epub 2011 Aug 26. PMID: 21873404
[14] Russell AB, Hood RD, Bui NK, et al. Type VI secretion delivers bacteriolytic effectors to target cells. Nature. 2011 Jul 20;475(7356):343-7. doi: 10.1038/nature10244. PMID: 21776080
[15] Osipiuk J, Xu X, Cui H, et al. Crystal structure of secretory protein Hcp3 from Pseudomonas aeruginosa. J Struct Funct Genomics. 2011 Mar;12(1):21-6. doi: 10.1007/s10969-011-9107-1. Epub 2011 Apr 8. PMID: 21476004
[16] Barret M, Egan F, Fargier E, et al. Genomic analysis of the type VI secretion systems in Pseudomonas spp.: novel clusters and putative effectors uncovered. Microbiology (Reading). 2011 Jun;157(Pt 6):1726-1739. doi: 10.1099/mic.0.048645-0. Epub 2011 Apr 7. PMID: 21474537
[17] Hachani A, Lossi NS, Hamilton A, et al. Type VI secretion system in Pseudomonas aeruginosa: secretion and multimerization of VgrG proteins. J Biol Chem. 2011 Apr 8;286(14):12317-27. doi: 10.1074/jbc.M110.193045. Epub 2011 Feb 16. PMID: 21325275
[18] Bleves S, Viarre V, Salacha R, et al. Protein secretion systems in Pseudomonas aeruginosa: A wealth of pathogenic weapons. Int J Med Microbiol. 2010 Dec;300(8):534-43. doi: 10.1016/j.ijmm.2010.08.005. Epub 2010 Oct 13. PMID: 20947426
[19] Mougous JD, Cuff ME, Raunser S, et al. A virulence locus of Pseudomonas aeruginosa encodes a protein secretion apparatus. Science. 2006 Jun 9;312(5779):1526-30. PMID: 16763151
[20] Robb CS, Assmus M, Nano FE, et al. Structure of the T6SS lipoprotein TssJ1 from Pseudomonas aeruginosa. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):607-10. doi: 10.1107/S1744309113012220. Epub 2013 May 23. PMID: 23722835
[21] Lu D, Shang G, Yu Q, et al. Expression, purification and preliminary crystallographic analysis of the T6SS effector protein Tse3 from Pseudomonas aeruginosa. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May 1;69(Pt 5):524-7. doi: 10.1107/S1744309113007148. Epub 2013 Apr 30. PMID: 23695568
[22] Basler M, Ho BT, Mekalanos JJ. Tit-for-tat: type VI secretion system counterattack during bacterial cell-cell interactions. Cell. 2013 Feb 14;152(4):884-94. doi: 10.1016/j.cell.2013.01.042. PMID: 23415234
[23] Hood RD, Singh P, Hsu F, et al. A type VI secretion system of Pseudomonas aeruginosa targets a toxin to bacteria. Cell Host Microbe. 2010 Jan 21;7(1):25-37. doi: 10.1016/j.chom.2009.12.007. PMID: 20114026
[24] Whitney JC, Beck CM, Goo YA, et al. Genetically distinct pathways guide effector export through the type VI secretion system. Mol Microbiol. 2014 May;92(3):529-42. doi: 10.1111/mmi.12571. Epub 2014 Mar 28. PMID: 24589350
[25] Hachani A, Allsopp LP, Oduko Y, et al. The VgrG proteins are "à la carte" delivery systems for bacterial type VI effectors. J Biol Chem. 2014 Jun 20;289(25):17872-84. doi: 10.1074/jbc.M114.563429. Epub 2014 May 2. PMID: 24794869
[26] Mougous JD, Gifford CA, Ramsdell TL, et al. Threonine phosphorylation post-translationally regulates protein secretion in Pseudomonas aeruginosa. Nat Cell Biol. 2007 Jul;9(7):797-803. Epub 2007 Jun 10. PMID: 17558395
[27] Hsu F, Schwarz S, Mougous JD. TagR promotes PpkA-catalysed type VI secretion activation in Pseudomonas aeruginosa. Mol Microbiol. 2009 Jun;72(5):1111-25. doi: 10.1111/j.1365-2958.2009.06701.x. Epub 2009 Apr 21. PMID: 19400797
[28] Förster A, Planamente S, Manoli E, et al. Coevolution of the ATPase ClpV, the sheath proteins TssB and TssC, and the accessory protein TagJ/HsiE1 distinguishes type VI secretion classes. J Biol Chem. 2014 Nov 21;289(47):33032-43. doi: 10.1074/jbc.M114.600510. Epub 2014 Oct 10. PMID: 25305017
experimental Experimental investigation has been performed on this T6SS
External database links

Locus tag (Gene)
Coordinate (Strand) 293802..296861 (-)
NCBI ID NP_248953.1
RefSeq NC_002516
Uniprot ID VGR2B_PSEAE
KEGG ID pae:PA0262
PDB ID 6H56
Pfam domain hit(s)

Domain Pfam ID E-value Aligned region
Transmembrane helices

  • Transmembrane helices are predicted using TMHMM 2.0 software.

Prediction                 Region     Sequence
Outside 1-1019 MRQRDLKFTFVVGEGKLAFDVVEFELEEALCEPFRLNLKLASDKNAIDFKQVLDQPGTFTLWQDGRPARYVHGIVSHFTQGSSGFRRTRYELLLEPQLARLELCCNWRIFQEKSVPEILQALLKEHRVLDYEQRIYHEHLPREYCVQAGDSDHYLHDRLAFEEGLVYYFRFDEHRHTLVCSDRLYVQERIAGGPVLFSAQPEGDNPQPVLHSFRYSENVRTARQTQRDYSFKRPTYDQEHHLAGEALEHQGSSYERYDYPGRYKRSGAGRPFTESRLRGHRRDARVASVSGDDPRLIPGHAFALEGHPRADFNAWWRPVRVVHRGTQYAGQEEESADAPLGVSYDLRAELVPEDVEWRPAPLPRPRIDGPQIATVVGPAGEEIHCDEWGRVKVQFPWDREGRHDEFSTCWIRVAQNWAGADWGHMAIPRIGQEVIVDYLDGDCDQPIVTGRTYRATNRPPYALPDHKILSTIKSKEYKGSRANELRIDDTTAQISAALMSDHGASALHLGYLTHPRPEGGKPRGEGFELRTDEHGAVRAAKGLLLSTEEQLRAGAGHLDRGVVVQVLEAALELARELGDYAGEHQGVGHDAAPQQTLQEAVRDLGHGANDESGKSNGGKPAIALSGPAGIAAATPASLTLAAGEHVDSVARQNQQVTAGQKVVINAGSDIGLFAQGGELRQITHQGPMLLQAQKNDIRLEAKQSVEVSASQQHVLVTAKEHITLMCGGAYLTLKGGNIELGMPGNFVVKAAKHSHVGAASLEAELPQFEVGETQRRFVLKQLDGQTAMPNVPYTITMANGEVIEGVTDAEGATQLLQKDAMNIAKVDMKHTKSPASAVAGIAAAVGAAVAVGKLLGGPDAEAGRALSEGEISLAKGVFGDSIDYSTVRLRDEDYVPWQGKDYVMAPNGHIYFGEELRGVADWSLESLQRQGLFIHEMTHVWQHQHGVNVLLVGAYQQARQFLLGDQYAYRLEPGKTLKDYNIEQQGDIVRDYFLEKNEFGEASANSRFAGVLKNFPTGY


Signal peptides
  • Sec/SPI: "standard" secretory signal peptides transported by the Sec translocon and cleaved by Signal Peptidase I (Lep).
  • Sec/SPII: lipoprotein signal peptides transported by the Sec translocon and cleaved by Signal Peptidase II (Lsp).
  • Tat/SPI: Tat signal peptides transported by the Tat translocon and cleaved by Signal Peptidase I (Lep).
Prediction        Probability Cleavage site Signal peptide sequence
Other 0.9855 - -


  Protein sequence: 1020 a.a.    


  Nucleotide sequence: 3060 bp