Protein Family Models

This entry represents the amino terminal three helical transmembrane region found in the CdaA diadenylate cyclase enzyme [1]. [1]. 26240071. An Essential Poison: Synthesis and Degradation of Cyclic Di-AMP. in Bacillus subtilis.. Gundlach J, Mehne FM, Herzberg C, Kampf J, Valerius O, Kaever V,. Stulke J;. J Bacteriol. 2015;197:3265-3274. (from Pfam)

Date:

2024-08-14

The DisA protein is a bacterial checkpoint protein that dimerises into an octameric complex. The protein consists of three distinct domains. This domain is the first and is a globular, nucleotide-binding region; the next 146-289 residues constitute the DisA-linker family, Pfam:PF10635, that consists of an elongated bundle of three alpha helices (alpha-6, alpha-10, and alpha-11), one side of which carries an additional three helices (alpha7-9), which thus forms a spine like-linker between domains 1 and 3. The C-terminal residues, of domain 3, are represented by family HHH, Pfam:PF00633, the specific DNA-binding domain. The octameric complex thus has structurally linked nucleotide-binding and DNA-binding HhH domains and the nucleotide-binding domains are bound to a cyclic di-adenosine phosphate such that DisA is a specific di-adenylate cyclase. This N-terminal domain has been identified as a diadenylate cyclase (DAC) responsible for producing c-di-AMP from two molecules of ATP [1]. The di-adenylate cyclase activity is strongly suppressed by binding to branched DNA, but not to duplex or single-stranded DNA, suggesting a role for DisA as a monitor of the presence of stalled replication forks or recombination intermediates via DNA structure-modulated c-di-AMP synthesis [2]. [1]. 32095817. Cyclic di-AMP, a second messenger of primary importance:. tertiary structures and binding mechanisms.. He J, Yin W, Galperin MY, Chou SH;. Nucleic Acids Res. 2020 Feb 25. pii: 5755; [Epub ahead of print]. [2]. 18439896. Structural biochemistry of a bacterial checkpoint protein. reveals diadenylate cyclase activity regulated by DNA. recombinat. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

diadenylate cyclase catalyzes the condensation of 2 ATP molecules into cyclic di-AMP

Date:

2021-01-21

CdaA (DacA), one class of diadenylate cyclase (also called cyclic-di-AMP synthase), produces cyclic di-3',5'-adenylate, a second messenger.

Gene:

cdaA

Date:

2024-05-30