UniProt functional annotation for O35002

UniProt code: O35002.

Organism: Bacillus subtilis (strain 168).
Taxonomy: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
 
Function: Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. {ECO:0000269|PubMed:14526016, ECO:0000269|PubMed:16818230, ECO:0000269|PubMed:17557826, ECO:0000269|PubMed:24243021}.
 
Catalytic activity: Reaction=The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.; EC=3.4.21.102; Evidence={ECO:0000269|PubMed:24243021};
Activity regulation: Activated by peptide binding to the PDZ domain. {ECO:0000269|PubMed:24243021}.
Subunit: Homodimer. {ECO:0000269|PubMed:24243021}.
Subcellular location: Forespore intermembrane space {ECO:0000269|PubMed:17557826}. Note=Is expressed in both the mother cell and forespore compartments but that synthesis in the forespore is both necessary and sufficient for the proper timing of pro-sigma-K processing.
Developmental stage: Is expressed in the forespore under the control of sigma-G, and in the mother cell under the control of sigma-E. {ECO:0000269|PubMed:14526016, ECO:0000269|PubMed:17557826}.
Domain: The PDZ domain functions as a gatekeeper to the protease tunnel and defines resting and active conformations of the protease. {ECO:0000269|PubMed:24243021}.
Ptm: Is cleaved by SpoIVB in vitro and in vivo but this cleavage does not appear to be necessary for CtpB activation. CtpB can also cleave itself in vivo. {ECO:0000269|PubMed:17557826, ECO:0000269|PubMed:24243021}.
Disruption phenotype: Pro-sigma-K processing is delayed by approximately 30 minutes, and sporulation efficiency is reduced approximately two-fold. {ECO:0000269|PubMed:14526016, ECO:0000269|PubMed:16818230, ECO:0000269|PubMed:24243021}.
Similarity: Belongs to the peptidase S41A family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.