| IED ID | IndEnz0002005899 |
| Enzyme Type ID | protease005899 |
| Protein Name |
Carboxypeptidase T EC 3.4.17.18 |
| Gene Name | cpt |
| Organism | Thermoactinomyces vulgaris |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Thermoactinomycetaceae Thermoactinomyces Thermoactinomyces vulgaris |
| Enzyme Sequence | MRKKWLSLSLVLVLIVACVPALGFSQNIENPSIFDLGIKLYKIDGVSTKEQRSAIASTGAAIEEVGKDYVKVLATPSEAKQIKQKGFTATVDTSLTTQDFPSYDSGYHNYNEMVNKINTVASNYPNIVKKFSIGKSYEGRELWAVKISDNVGTDENEPEVLYTALHHAREHLTVEMALYTLDLFTQNYNLDSRITNLVNNREIYIVFNINPDGGEYDISSGSYKSWRKNRQPNSGSSYVGTDLNRNYGYKWGCCGGSSGSPSSETYRGRSAFSAPETAAMRDFINSRVVGGKQQIKTLITFHTYSELILYPYGYTYTDVPSDMTQDDFNVFKTMANTMAQTNGYTPQQASDLYITDGDMTDWAYGQHKIFAFTFEMYPTSYNPGFYPPDEVIGRETSRNKEAVLYVAEKADCPYSVIGKSCSTK |
| Enzyme Length | 424 |
| Uniprot Accession Number | P29068 |
| Absorption | |
| Active Site | ACT_SITE 375; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:1521526 |
| Activity Regulation | ACTIVITY REGULATION: Binds four calcium ions which seem to play an important role in the thermostability of the enzyme. {ECO:0000305|PubMed:1521526}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Releases a C-terminal residue, which may be hydrophobic or positively charged.; EC=3.4.17.18; |
| DNA Binding | |
| EC Number | 3.4.17.18 |
| Enzyme Function | FUNCTION: Able to split off hydrophobic and basic amino acids with comparable efficiency. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (10); Chain (1); Disulfide bond (2); Helix (14); Metal binding (3); Propeptide (1); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Calcium;Carboxypeptidase;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (23) |
| Cross Reference PDB | 1OBR; 3PRT; 3QNV; 3V38; 3V7Z; 4DJL; 4DUK; 4F8Z; 4GM5; 4IAV; 4IHM; 4IK2; 6F6Q; 6F75; 6F79; 6GO2; 6Q4L; 6SN6; 6T9Y; 6TNK; 6Z28; 7AQP; 7ARU; |
| Mapped Pubmed ID | 23586718; 25619204; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,476 |
| Kinetics | |
| Metal Binding | METAL 167; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:1521526; METAL 170; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:1521526; METAL 302; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:1521526 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.18; |