| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
1.A.34.1.1 | 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. | Bacteria |
Bacillota | The SpoIIQ/SpoIIIAH complex of Bacillus subtilis SpoIIQ (P71044) SpoIIIAH (P49785) |
|
1.A.34.1.2 | 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. | Bacteria |
Pseudomonadota | SpoIIQ homologue of E. coli |
|
1.A.34.1.3 | Uncharacterized metaloprotease family M23 of 245 aas. Shows sequence similarity to SpoIIQ in an 80 residue region, residues 140 - 220 in both proteins. | Bacteria |
Pseudomonadota | UP of E. coli |
|
1.A.34.1.4 | SpoIIQ-SpoIIIAH complex spanning the two membranes of the mother cell and the prespore. Inhibiting SpoIIQ, SpoIIIAA, or SpoIIIAH function apparently prevents the formation of infectious C. difficile spores and thus disease transmission (Fimlaid et al. 2015). spoIIQ or spoIIIAH mutants that complete engulfment are impaired in post-engulfment, forespore and mother cell-specific gene expression, in agreement with a channel-like function (Serrano et al. 2016). | Bacteria |
Bacillota | SpoIIQ-SpoIIIAH of Clostridium difficile SpoIIQ, 222 aas and 1 N-terminal TMS SpoIIIAH, 229 aas and 1 N-terminal TMS |