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Literature summary for 2.7.7.85 extracted from

  • Zheng, C.; Ma, Y.; Wang, X.; Xie, Y.; Ali, M.K.; He, J.
    Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensis (2015), Front. Microbiol., 6, 908.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.85

Protein Variants

Protein Variants Comment Organism
additional information deletion of the N-terminal YojJ domain leads to complete loss of activity. Truncated proteins CdaS28-201, CdaS17-201, and CdaS11-201 show no diadenylate cyclase activity and CdaS10-201, CdaS9-201, CdaS8-201, CdaS7-201, and CdaS5-201 have only weak activity, while CdaS4-201 activity is comparable with wild type CdaS Bacillus thuringiensis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ best activator, maximum activity at 10 mM Bacillus thuringiensis
additional information activity is strictly dependent on divalent cations Bacillus thuringiensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
22000
-
-
 Bacillus thuringiensis
23300
-
-
 Bacillus thuringiensis
155000
-
 gel filtration Bacillus thuringiensis

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis D5TM67
-
-
Bacillus thuringiensis BMB171 D5TM67
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ADP
-
 Bacillus thuringiensis ? + cyclic di-3',5'-adenylate ADP is partially converted to cyclic di-AMP, but the yield is lower compared with that using ATP as the substrate ?
2 ADP
-
 Bacillus thuringiensis BMB171 ? + cyclic di-3',5'-adenylate ADP is partially converted to cyclic di-AMP, but the yield is lower compared with that using ATP as the substrate ?
2 ATP
-
 Bacillus thuringiensis 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2 ATP
-
 Bacillus thuringiensis BMB171 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
additional information enzyme displays weak ADPase activity Bacillus thuringiensis ?
-
 ?
additional information enzyme displays weak ADPase activity Bacillus thuringiensis BMB171 ?
-
 ?

Subunits

Subunits Comment Organism
hexamer 6 * 22000, SDS-PAGe, 6 * 23300, calculated Bacillus thuringiensis

Synonyms

Synonyms Comment Organism
CdaS
-
 Bacillus thuringiensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Bacillus thuringiensis

General Information

General Information Comment Organism
physiological function transcription of CdaS is initiated by the sporulation-specific sigma factor sigma(H) and the deletion of CdaS significantly delays sporulation and parasporal crystal formation. Deletion of all the three diadenylate cyclase genes from a single strain is unsuccessful Bacillus thuringiensis