Part:BBa_K1639008
Tev Protease, single S219V mutation in the internal cleavage site
TEV protease (also called Tobacco Etch Virus nuclear inclusion a endopeptidase) is a highly sequence-specific cysteine protease from Tobacco Etch Virus (TEV).The consensus for these native cut sites is ENLYFQ\S where ‘\’ denotes the cleaved peptide bond.One of the main uses of this protein is for removing affinity tags from purified proteins. The reason for the use of TEV protease as a biochemical tool is its high sequence specificity. This specificity allows for the controlled cleavage of proteins when the preference sequence is inserted into flexible loops. It also makes it relatively non-toxic in vivo as the recognized sequence scarcely occurs in proteins.[1]
PotB59, chimeric protein that is formed by the N-terminal region of PomB and the C-terminal of E. Coli MotB
It was shown that a chimeric protein, PotB, renamed as PotB59, that has the N-terminal region of PomB (1–50) fused to the C-terminal periplasmic region of E. coli MotB (59–308), is functional with PomA in E. coli as well as in strains of V. alginolyticus that are defective in MotX or MotY (Asai et al. 2003) Instead of the hydrogen-dependent MotA, MotB stator protein partially adapted from the V. alginolyticus, sodium-dependent Stator proteins were insalled. After this adaptation, the flagellar velocity increased by twice fold.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 2
Illegal XhoI site found at 744 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 605
//chassis/prokaryote/ecoli
//collections/probiotics/production
| n/a | Tev Protease, single S219V mutation in the internal cleavage site |