| IED ID | IndEnz0002003457 |
| Enzyme Type ID | protease003457 |
| Protein Name |
Carboxy-terminal processing protease CtpB C-terminal processing protease EC 3.4.21.102 |
| Gene Name | ctpB yvjB BSU35240 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MNQKIMAVIAAGSMLFGGAGVYAGINLLEMDKPQTAAVPATAQADSERDKAMDKIEKAYELISNEYVEKVDREKLLEGAIQGMLSTLNDPYSVYMDKQTAKQFSDSLDSSFEGIGAEVGMEDGKIIIVSPFKKSPAEKAGLKPNDEIISINGESMAGKDLNHAVLKIRGKKGSSVSMKIQRPGTKKQLSFRIKRAEIPLETVFASEKKVQGHSVGYIAISTFSEHTAEDFAKALRELEKKEIEGLVIDVRGNPGGYLQSVEEILKHFVTKDQPYIQIAERNGDKKRYFSTLTHKKAYPVNVITDKGSASASEILAGALKEAGHYDVVGDTSFGKGTVQQAVPMGDGSNIKLTLYKWLTPNGNWIHKKGIEPTIAIKQPDYFSAGPLQLKEPLKVDMNNEDVKHAQVLLKGLSFDPGREDGYFSKDMKKAVMAFQDQNKLNKTGVIDTRTAETLNQQIEKKKSDEKNDLQLQTALKSLFVN |
| Enzyme Length | 480 |
| Uniprot Accession Number | O35002 |
| Absorption | |
| Active Site | ACT_SITE 309; /note=Nucleophile; /evidence=ECO:0000269|PubMed:24243021; ACT_SITE 334; /note=Charge relay system; /evidence=ECO:0000269|PubMed:24243021; ACT_SITE 338; /note=Charge relay system; /evidence=ECO:0000269|PubMed:24243021 |
| Activity Regulation | ACTIVITY REGULATION: Activated by peptide binding to the PDZ domain. {ECO:0000269|PubMed:24243021}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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}; |
| DNA Binding | |
| EC Number | 3.4.21.102 |
| Enzyme Function | 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}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (22); Chain (1); Domain (1); Helix (14); Mutagenesis (6); Region (1); Signal peptide (1); Site (4); Turn (3) |
| Keywords | 3D-structure;Autocatalytic cleavage;Hydrolase;Protease;Reference proteome;Serine protease;Signal;Sporulation |
| Interact With | Itself; P26936 |
| Induction | |
| Subcellular Location | 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. |
| Modified Residue | |
| Post Translational Modification | 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}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 4C2C; 4C2D; 4C2E; 4C2F; 4C2G; 4C2H; |
| Mapped Pubmed ID | 21630458; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,798 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.102; |