Detailed information of component protein
Summary
| Component ID |
T6CP259501 |
| Component protein type |
PAAR |
| T6SS ID (Type) |
T6SS00005 (Type i4a) |
| Strain |
Pseudomonas aeruginosa PAO1 |
| Replicon |
chromosome (H3-T6SS) |
| Sequence |
Protein sequence (132 a.a.); Nucleotide sequence (396 bp) |
| Reference |
[1] 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[2] 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[3] 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[4] 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[5] 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[6] Sana TG, Soscia C, Tonglet CM, et al. Divergent control of two type VI secretion systems by RpoN in Pseudomonas aeruginosa. PLoS One. 2013 Oct 21;8(10):e76030. doi: 10.1371/journal.pone.0076030. eCollection 2013. PMID: 24204589[7] Jiang F, Waterfield NR, Yang J, et al. A Pseudomonas aeruginosa type VI secretion phospholipase D effector targets both prokaryotic and eukaryotic cells. Cell Host Microbe. 2014 May 14;15(5):600-10. doi: 10.1016/j.chom.2014.04.010. PMID: 24832454[8] Chen Z, Gao Z, Hu H, et al. Cloning, purification, crystallization and preliminary X-ray studies of the putative type VI secretion immunity protein Tli5 (PA5088) from Pseudomonas aeruginosa. Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):903-5. doi: 10.1107/S2053230X14010164. Epub 2014 Jun 18. PMID: 25005085 |

Experimental investigation has been performed on this T6SS
External database links
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 |
1-131 |
MSGKPAARLGDPTACPLPGHGSNPIVGGSPDVFFDHLSAARQGDATACGATLSANVIANVLINGKPATVVGSVGTHGNLVVGGAGTVLIGNSGGGAPALALAPPKLCLQCLLLAARRNQALVPLESLGGAP |
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 |
0.9362 |
- |
- |
Protein sequence: 132 a.a.
Nucleotide sequence: 396 bp