Bacterial virus anti-defence systems · sequence & structure resource

Encyclopaedia of Bacterial Virus Anti-Defence Systems


Protein: NARP1_Adps (ADPR-PP synthetase)

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Overview

Mode of Action (MoA) adds a pyrophosphate group from ATP to ADPR to create ADPR-PP
Evidence Expression of Adps homolog from phage SpβL1 produced ADPR-PP from ADPR and ATP in vitro. Mass spectrometry (MS/MS) confirmed the identity of the reaction products (ADPR-PP and ADPR-cyclic phosphate, ECO_0001096). Mutation of a key active site residue (K162A) abolished activity, showing the importance of this residue (ECO_0000015).
MoA Category synthesises and restores essential molecules depleted by bacterial defence
Subtype(s) of the defence system(s) inhibited by the protein Defence Subtype Bacillus subtilis type I Thoeris, DSR1, DSR2 and SEFIR. Escherichia coli SIR2–HerA
Relevant publication(s) DOI 10.1038/s41586-024-07986-w
Other components of the anti-defence system Multicomponent System namat
Known structure in PDB PDB ID -
Genome(s) encoding the protein Protein Source Escherichia phage JohannRWettstein (Bas63)
Defence system(s) inhibited by the protein Defences Thoeris, DSR, SIR2-HerA, SEFIR

3D structure

AlphaFold 3 model.

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Feature viewer - predicted secondary structure

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Pfam annotations

Pfam Name Pfam Acc Pfam Length Colour HMM Start HMM End Ali Start Ali End Env Start Env End Evalue
Pribosyltran PF00156 158 30 124 160 249 131 276 8.3e-14
Pribosyl_synth PF14572 184 64 147 191 275 162 289 2.5e-12

Sequence Viewer

Amino acid position: -

MKTVIEAVVTAQEKFFHTEKFNIIQFPSGEIGGNFSEDFVKFTERNAGKIDNVIITVQGYDKDTLFALALAKDAVDSLVPQKSAMKTIVFGFLPNARYDRHMFKGDAAALKVFANLVNAMGFDAVCALDPHSNVAENLFKCFQSMKQKDVAVHFASDPRIDFLVAPDAGAAKKTEDTAKEVDKPYITMSKVRNLKTGEITGMRILDDVDLTDKTVMILDDICDGGRTFVEAAKHLREAGAKRVELYVTHGIFSKGVENLLDNGIDHIYTTNTLGEAKDRGLTHYGQVTVATID