GAPS6

Contributors: Jean Cury

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:

gaps6

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