Literature summary for 2.7.13.3 extracted from

Geiger, C.; Spiess, T.; Korn, S.; Koetter, P.; Entian, K.
Specificity of subtilin-mediated activation of histidine kinase SpaK (2017), Appl. Environ. Microbiol., 83, e00781 .

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Activating Compound

Activating Compound	Comment	Organism	Structure
subtilin	subtilin activates the two-component system SpaRK of Bacillus subtilis to autoinduce its biosynthesis. Amino acid position 20 is crucial for SpaK activation by subtilin. An engineered nisin molecule with phenylalanine at position 20 (nisin N20F) is able to activate SpaK in a specific manner. In combination with the N-terminal tryptophan of subtilin (nisin I1W/N20F), SpaK autoinduction reaches almost the level of subtilin-mediated autoinduction. The overall structure of subtilin is also important for its association with the histidine kinase. The destruction of the second lanthionine ring (subtilin C11A, ring B), as well as mutations that interfere with the flexibility of the hinge region located between lanthionine rings C and D (subtilin L21P/Q22P), abolish SpaK autoinduction. The C-terminal part of subtilin is needed for efficient SpaK autoinduction, but the destruction of lanthionine rings D and E has no measurable impact	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P33113	-	-

Synonyms

Synonyms	Comment	Organism
SPAK	-	Bacillus subtilis

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Release 2023.1 (January 2023)