P0DXA6 · CDNE_STASC
- ProteinCyclic GMP-AMP synthase CdnE03
- GenecdnE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids324 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:37968393).
CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage (PubMed:37968393).
The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals (PubMed:37968393).
The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (PubMed:37968393).
The effector for this system is downstream Cap15 (PubMed:37968393).
A type I-B CBASS system (PubMed:32839535).
CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage (PubMed:37968393).
The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals (PubMed:37968393).
The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (PubMed:37968393).
The effector for this system is downstream Cap15 (PubMed:37968393).
A type I-B CBASS system (PubMed:32839535).
Cyclic dinucleotide synthase that catalyzes the synthesis of 3',2'-cyclic GMP-AMP (cGAMP) from GTP and ATP upon activation by viral-derived cabRNA (PubMed:37968393).
Binds cabRNA via positive charges in its N-terminus (PubMed:37968393).
Binds cabRNA via positive charges in its N-terminus (PubMed:37968393).
Protects S.aureus against phage infection. When the CBASS operon (cdnE-cap15) is introduced in S.aureus strain RN4220 there is strong protection against lytic DNA phages 80alpha-vir and phi-NM1-gamma-6 but little to no protection against phages phi-NM4-gamma-4 or phi-12-gamma-3 (PubMed:37968393).
Catalytic activity
- GTP + ATP = 3',2'-cGAMP + 2 diphosphateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Activity regulation
Activated by a virus-derived, approximately 400 nucleotide RNA (called CBASS-activating bacteriophage RNA, cabRNA) that begins in the viral terminase subunit terS and extends into terL (PubMed:37968393).
RNA secondary and/or tertiary structure, as well as viral infection itself, are important for CdnE activation (PubMed:37968393).
A much longer RNA (escaper RNA) with a different secondary structure, derived from a terS-mutated virus still binds to this protein, but does not activate its nucleotide cyclase activity (PubMed:37968393).
Shorter viral-derived RNAs (34 and 49 nt) with extensive predicted secondary structure also activate the enzyme, although not as well as full-length cabRNA (PubMed:37968393).
RNA secondary and/or tertiary structure, as well as viral infection itself, are important for CdnE activation (PubMed:37968393).
A much longer RNA (escaper RNA) with a different secondary structure, derived from a terS-mutated virus still binds to this protein, but does not activate its nucleotide cyclase activity (PubMed:37968393).
Shorter viral-derived RNAs (34 and 49 nt) with extensive predicted secondary structure also activate the enzyme, although not as well as full-length cabRNA (PubMed:37968393).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 87 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 89 | ATP (UniProtKB | ChEBI) | |||
Binding site | 89 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 144-145 | ATP (UniProtKB | ChEBI) | |||
Binding site | 159 | ATP (UniProtKB | ChEBI) | |||
Binding site | 159 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 224 | GTP (UniProtKB | ChEBI) | |||
Binding site | 243 | GTP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | GTP binding | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotidyltransferase activity | |
Molecular Function | RNA binding | |
Biological Process | defense response to virus |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCyclic GMP-AMP synthase CdnE03
- EC number
- Short namesSsc-CdnE03
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionP0DXA6
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 9 | Does not make cyclic 3',2'-cGAMP (3',2'-cGAMP), does not bind cabRNA, does not protect against phage. | |||
Mutagenesis | 13 | Substantially reduces synthesis of 3',2'-cGAMP, weakly binds cabRNA, reduced protection against phage. | |||
Mutagenesis | 87-89 | Does not protect against phage, does not make 3',2'-cGAMP. | |||
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000459831 | 1-324 | Cyclic GMP-AMP synthase CdnE03 | ||
Family & Domains
Sequence
- Sequence statusComplete
- Length324
- Mass (Da)38,298
- Last updated2024-03-27 v1
- ChecksumB96161166556485F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP009762 EMBL· GenBank· DDBJ | AKS70342.1 EMBL· GenBank· DDBJ | Genomic DNA |