Literature summary for 2.7.7.65 extracted from

Angerer, V.; Schwenk, P.; Wallner, T.; Kaever, V.; Hiltbrunner, A.; Wilde, A.
The protein Slr1143 is an active diguanylate cyclase in Synechocystis sp. PCC 6803 and interacts with the photoreceptor Cph2 (2017), Microbiology, 163, 920-930 .

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Protein Variants

Protein Variants	Comment	Organism
additional information	generation of knockout DELTAslr1143 mutants of Cph2. Whereas wild-type cells are non-motile under high-intensity red light of 640 nm, the mutant DELTAslr1143 displays positive phototaxis. This phenotype can be complemented by overexpression of full-length Slr1143, which also results in an increased cellular c-di-GMP concentration. However, the non-motile phenotype of wild-type cells under high-intensity red light appears not to be due to an elevated cellular c-di-GMP content	Synechocystis sp. PCC 6803

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2 GTP	Synechocystis sp. PCC 6803	-	2 diphosphate + cyclic di-3',5'-guanylate	-	?

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp. PCC 6803	P73272	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 GTP	-	Synechocystis sp. PCC 6803	2 diphosphate + cyclic di-3',5'-guanylate	-	?

Synonyms

Synonyms	Comment	Organism
Slr1143	-	Synechocystis sp. PCC 6803

General Information

General Information	Comment	Organism
malfunction	mutation of gene slr1143 results in an aberrant phototactic behaviour in red light. DELTAslr1143 and Slr1143 overexpression mutant lines in different light qualities suggesting that motility of Synechocystis cells can be affected by the cellular levels of c-di-GMP, but this appears to not be the exclusive reason for differences in motility	Synechocystis sp. PCC 6803
additional information	in blue light, wild-type cells are sessile while DELTAcph2 cells move towards the light source. The product of the gene cph2 is a photosensory protein, Cph2, which consists of six domains with the architecture GAF-GAF-GGDEF-EAL-CBCR-GGDEF (GAF, cGMP phosphodiesterase/adenylyl cylase/FhlA, CBCR, cyanobacteriochrome, GGDEF, degenerate motif). The domains 1 (GAF) and 5 (CBCR) covalently bind phycocyanobilin (PCB) as a chromophore, allowing the absorbance of light in the visible spectrum	Synechocystis sp. PCC 6803
physiological function	the second messenger cyclic dimeric guanosine monophosphate (c-di-GMP) is ubiquitous in bacteria. It is synthesized from two molecules of GTP by diguanylate cyclases (DGCs), which possess the c-di-GMP synthesis GGDEF domain. In the unicellular cyanobacterium Synechocystis sp. PCC 6803 (Synechocystis) c-di-GMP influences the decision between motility and sessility. The photoreceptor Cph2 from the cyanobacterium Synechocystis sp. PCC 6803 comprises three domains related to c-di-GMP metabolism: two GGDEF and one EAL domain. It has been shown that the C-terminal GGDEF domain acts as blue-light triggered c-di-GMP producer thereby inhibiting motility of the cells in blue light. Binding of Cph2 and Slr1143 is likely mediated through interaction of Cph2 with the GGDEF domain of Slr1143, the interaction is not stoichiometric. Analysis of protein-protein interaction of Slr1143 with Cph2, overview	Synechocystis sp. PCC 6803

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Release 2023.1 (January 2023)