GAPS6

Description

GAPS (GMT-encoded Anti-Phage System) antiphage systems were discovered on newly described Gamma-Mobile-Trio elements.

GAPS6 is composed of two proteins, GAPS6a and GAPS6b. These two proteins are encoded together in diverse Gram-negative bacteria.

Molecular mechanism

GAPS6b is essential for the defense phenotype, however it is not known whether GAPS6b could be sufficient. GAPS6b is composed of TPR repeats at the N-terminus, possibly allowing ligand binding and a predicted RNAse domain (PINc, PF08745.14) at the C-terminus. PINc domains have been implicated as toxins in bacterial toxin-antitoxin modules (N/A) . The PINc domain is required for the anti-phage defense activity of GAPS6.

Example of genomic structure

The GAPS6 is composed of 2 proteins: GAPS6a and GAPS6b.

Here is an example found in the RefSeq database:

The GAPS6 system in Escherichia coli (GCF_013372365.1, NZ_CP054227) is composed of 2 proteins GAPS6b (WP_096985931.1) GAPS6a (WP_000346990.1)

Distribution of the system among prokaryotes

Structure

Experimental validation

      
graph LR;
    Mahata_2023[Mahata et al., 2023] --> Origin_0
    Origin_0[Vibrio parahaemolyticus 
WP_248387294.1, WP_248387295.1] --> Expressed_0[Escherichia coli]
    Expressed_0[Escherichia coli] ----> T7 & T4 & P1-vir & Lambda-vir
    subgraph Title1[Reference]
        Mahata_2023
end
    subgraph Title2[System origin]
        Origin_0
end
    subgraph Title3[Expression species]
        Expressed_0
end
    subgraph Title4[Protects against]
        T4
        Lambda-vir
end
    style Title1 fill:none,stroke:none,stroke-width:none
    style Title2 fill:none,stroke:none,stroke-width:none
    style Title3 fill:none,stroke:none,stroke-width:none
    style Title4 fill:none,stroke:none,stroke-width:none