[1] The SOBER (Suppressor of AvrBsT-elicited resistance) 1 protein is conserved in plants and it suppresses the plant's ability to carry out the hypersensitive response against infection by certain pathogenic effector proteins from the YopJ family.

[2] SOBER1 belongs to the protein superfamily of α/β hydrolases and possesses a canonical serine/histidine/aspartate catalytic triad to carry out the deacetylation reaction.

There have been contradicting reports about SOBER1's potential phospholipase activity, with one study claiming phospholipase A2 activity of the protein[3] and another study being unable to reproduce this result.

[1] Members of the SOBER1 family are considered closely related to acyl-protein thioesterases, judged by their protein structure.

[2] However, a change in their amino acid sequence renders SOBER1's biochemical properties into a deacetylase; in particular the hydrophobic tunnel, which is found in acyl-protein thioesterases, is impaired by additional amino acids in the lid structure of SOBER1, creating a new surface for binding of the acetyl group.