Phosphoserine phosphatase SerB2
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
In the host, induces significant cytoskeleton rearrangements through cofilin dephosphorylation and its subsequent activation, and affects the expression of genes that regulate actin dynamics. It specifically interacts with HSP90, HSP70 and HSP27 that block apoptotic pathways but not with other HSPs. Also interacts with GAPDH. It actively dephosphorylates MAP kinase p38 and NF-kappa B p65 (specifically at Ser-536) that play crucial roles in inflammatory and immune responses. This in turn leads to down-regulation of Interleukin 8, a chemotactic and inflammatory cytokine. Thus might help the pathogen to evade the host's immune response (PubMed:26984196). Exogenous addition of purified SerB2 protein to human THP-1 cells (that can be differentiated into macrophage-like cells) induces microtubule rearrangements; the phosphatase activity is co-related to the elicited rearrangements, while addition of the ACT-domains alone elicits no rearrangements (PubMed:25521849).
Belongs to the HAD-like hydrolase superfamily. SerB family.