2kwa
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1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis
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Structural highlights
FunctionPXPB_BACSU Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate (PubMed:28830929). In addition, is a potent inhibitor of the autophosphorylation reaction of kinase A (kinA) and its reverse reaction, but does not inhibit phosphate transfer to the Spo0F response regulator once kinase A is phosphorylated. Is an inhibitor of the catalytic domain of kinase A affecting the ATP/ADP reactions and not the phosphotransferase functions of this domain. The inhibition is non-competitive with respect to ATP (PubMed:9334321).[1] [2] References
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This page was last modified 06:49, 1 May 2024.