1yav | pdb_00001yav
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Crystal structure of CBS domain-containing protein ykuL from Bacillus subtilis
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Structural highlights
FunctionDARB_BACSU Involved in the c-di-AMP-dependent regulation of the bacterial stringent response (PubMed:33619274, PubMed:35130724). Modulates the activities of at least two enzymes under conditions of potassium limitation (PubMed:33619274, PubMed:35130724). Apo-DarB regulates the activity of the GTP pyrophosphokinase RelA by interacting directly with RelA, leading to stimulation of (p)ppGpp synthesis and induction of the stringent response (PubMed:33619274). Apo-DarB also regulates pyruvate carboxylase (PYC) at two levels: directly at the protein level by binding to the enzyme and stimulating the synthesis of oxaloacetate and indirectly, by interaction with RelA, which leads to activation of the stringent response and to the increased expression of the pycA gene (PubMed:35130724). Stimulation of these enzymes by DarB is prevented in the presence of cyclic di-AMP (c-di-AMP) (PubMed:33619274, PubMed:35130724).[1] [2] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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This page was last modified 08:56, 14 February 2024.