Literature summary extracted from

Du, Y.; Shi, W.W.; He, Y.X.; Yang, Y.H.; Zhou, C.Z.; Chen, Y.
Structures of the substrate-binding protein provide insights into the multiple compatible solute binding specificities of the Bacillus subtilis ABC transporter OpuC (2011), Biochem. J., 436, 283-289.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
7.6.2.9	expression in Escherichia coli	Bacillus subtilis

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
7.6.2.9	substrate-binding protein OpuCC in the apo-form and in complex with carnitine, glycine betaine, choline and ectoine to 2.3, 2.7, 2.4, 1.9 and 2.1 A resolution, respectively. OpuCC is composed of two alpha/beta/alpha globular sandwich domains linked by two hinge regions, with a substrate-binding pocket located at the interdomain cleft. Upon substrate binding, the two domains shift towards each other to trap the substrate	Bacillus subtilis

Protein Variants

EC Number	Protein Variants	Comment	Organism
7.6.2.9	T94D	shares a quite similar pattern of fluorescence spectrum to that of the paralogue OpuBC. Only choline can trigger obvious changes of fluorescence intensity of mutant T94D, whereas carnitine, GB and ectoine cannot	Bacillus subtilis
7.6.2.9	Y91A	complete loss of binding affinity	Bacillus subtilis
7.6.2.9	Y91F	slight decrease in binding affinity	Bacillus subtilis
7.6.2.9	Y91W	slight decrease in binding affinity	Bacillus subtilis

Organism

EC Number	Organism	UniProt	Comment	Textmining
7.6.2.9	Bacillus subtilis	O32243	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
7.6.2.9	glycine betaine/carnitine/choline-binding protein	-	Bacillus subtilis
7.6.2.9	OpuCC	-	Bacillus subtilis

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Release 2023.1 (January 2023)