Detail Information for IndEnz0002005137
IED ID IndEnz0002005137
Enzyme Type ID protease005137
Protein Name Carboxy-terminal processing protease CtpA
C-terminal processing protease
EC 3.4.21.102
Gene Name ctpA orfRM1 BSU19590
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 MKRQLKLFFIVLITAVVASALTLFITGNSSILGQKSASTGDSKFDKLNKAYEQIKSDYYQKTDDDKLVDGAIKGMIQSLDDPYSTYMDQEQAKSFDETISASFEGIGAQVEEKDGEILIVSPIKGSPAEKAGIKPRDQIIKVNGKSVKGMNVNEAVALIRGKKGTKVKLELNRAGVGNIDLSIKRDTIPVETVYSEMKDNNIGEIQITSFSETTAKELTDAIDSLEKKGAKGYILDLRGNPGGLMEQAITMSNLFIDKGKNIMQVEYKNGSKEVMKAEKERKVTKPTVVLVNDGTASAAEIMAAALHESSNVPLIGETTFGKGTVQTAKEYDDGSTVKLTVAKWLTADGEWIHKKGIKPQVKAELPDYAKLPYLDADKTYKSGDTGTNVKVAQKMLKALGYKVKVNSMYDQDFVSVVKQFQKKEKLNETGILTGDTTTKLMIELQKKLSDNDTQMEKAIETLKKEM
Enzyme Length 466
Uniprot Accession Number O34666
Absorption
Active Site ACT_SITE 297; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 308; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 322; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
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;
DNA Binding
EC Number 3.4.21.102
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (1); Sequence conflict (1); Signal peptide (1)
Keywords Hydrolase;Protease;Reference proteome;Serine protease;Signal
Interact With
Induction INDUCTION: Is expressed only during vegetative growth. {ECO:0000269|PubMed:8996100}.
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..36; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 51,149
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda