Literature summary for 2.7.7.B22 extracted from

Nicolas, E.; Oger, C.A.; Nguyen, N.; Lambin, M.; Draime, A.; Leterme, S.C.; Chandler, M.; Hallet, B.F.
Unlocking Tn3-family transposase activity in vitro unveils an asymetric pathway for transposome assembly (2017), Proc. Natl. Acad. Sci. USA, 114, E669-E678 .

Search for more literature for 2.7.7.B22

Protein Variants

Protein Variants	Comment	Organism
A174V	substitution close to the putative N-terminal DNA-binding domain of TnpA, reduces immunity by approximately sixfold. Transposition activity is comparable to that of wild-type	Bacillus thuringiensis
E740G	C-terminal substitutions within the predicted RNaseH fold, reduces immunity up to about12fold. Transposition activity is comparable to that of wild-type	Bacillus thuringiensis
additional information	compared with wild-type TnpA, Tn4430 TnpA mutants that are proficient in transposition but impaired in target immunity exhibit deregulated activities. They spontaneously assemble a unique asymmetric synaptic complex in which one TnpA molecule simultaneously binds two transposon ends. In this complex, TnpA is in an activated state competent for DNA cleavage and strand transfer. Wild-type TnpA can form this complex only on precleaved ends mimicking the initial step of transposition	Bacillus thuringiensis
S911R	C-terminal substitution adjacent to the predicted RNaseH fold, reduces immunity up to about 25fold. Transposition activity is comparable to that of wild-type	Bacillus thuringiensis
W24R	substitution within the putative N-terminal DNA-binding domain of TnpA, reduces immunity by approximately twofold. Transposition activity is comparable to that of wild-type	Bacillus thuringiensis
W24R/A174V/E740G	triple mutant is hyperactive in vivo, giving elevated levels of transposition into both permissive and immune targets	Bacillus thuringiensis

Organism

Organism	UniProt	Comment	Textmining
Bacillus thuringiensis	P10021	-	-

Synonyms

Synonyms	Comment	Organism
Tn4430 TnpA	-	Bacillus thuringiensis
TnpA	-	Bacillus thuringiensis
transposase for transposon Tn4430	-	Bacillus thuringiensis

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Release 2023.1 (January 2023)