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The Bacillus SpoIIQ/SpoIIIAH transcompartment channel interconnects the forespore and the mother cell. The activity of sigmaG requires this channel apparatus through which the adjacent mother cell provides substrates that generally support gene expression in the forespore. Flanagan et al. 2016 reported that SpoIIQ is bifunctional, specifically maximizing sigmaG activity as part of a regulatory circuit that prevents sigmaG from activating transcription of the gene encoding its own inhibitor, the anti-sigma factor CsfB.

The SpoIIQ/SpoIIIAH complex of Bacillus subtilis
SpoIIQ (P71044)
SpoIIIAH (P49785)

SpoIIQ homologue of one of the two components (SpoIIQ and SpoIIIAH) of the gap junction-like channel-forming complex of B. subtilis.  Several SpoIIQ homologues in various E. coli strains were identified, but no homologue of the SpoIIAH component was found.  Therefore, pore formation can not be inferred.

SpoIIQ homologue of E. coli

Uncharacterized protein of 245 aas

UP of E. coli