Bacterial virus anti-defence systems · sequence & structure resource

Encyclopaedia of Bacterial Virus Anti-Defence Systems


Protein: ArdK

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Overview

Mode of Action (MoA) the mechanism is not clear, apart from its role in regulating the expression of ardA and ardB.
Evidence ArdK was identified as a transcriptional regulator of the antirestriction genes ardA and ardB through promoter activity assays and stability experiments using plasmid derivatives with and without upstream regulatory sequences. Expression of ardB from constructs containing the upstream conserved CUP region (e.g., pCAT66-4) resulted in plasmid instability unless ArdK was provided in trans, suggesting repression of a strong promoter (P2) by ArdK. Promoter probe assays showed that ArdK specifically repressed P2 activity but not P1. Maxicell experiments confirmed expression of a 15-kDa ArdK protein from the ardK gene. Combined with ArdR, ArdK completely abolished promoter activity from CUP sequences upstream of ardB and ardA, indicating coordinated repression at the transcriptional level. Sequence homology in the regulatory regions of ardA and ardB (94% identity) further supports ArdK’s dual role in their regulation.
MoA Category unknown
Subtype(s) of the defence system(s) inhibited by the protein Defence Subtype Escherichia coli type I RM
Relevant publication(s) DOI 10.1128/jb.175.15.4843-4850.1993
Other components of the anti-defence system Multicomponent System ardr; arda; ardc
Known structure in PDB PDB ID 7BBQ
Genome(s) encoding the protein Protein Source Plasmid pKM101
Defence system(s) inhibited by the protein Defences RM

3D structure

PDB entry model.

A similar PDB structure exists: 7BBQ

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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
KORA PF16509 84 3 82 9 93 7 95 7.2e-12

Sequence Viewer

Amino acid position: -

MAQKNRISETEWKQLLPQMASFAHITTDIGYSVLVKGEKSSDVATRVGRSKQNISSTVKRIWDLYQNTTLKAENGEPLKLVQVWIPASLAETVLKEAAKYSINNITTSEMEKK