| IED ID | IndEnz0002011580 |
| Enzyme Type ID | protease011580 |
| Protein Name |
Proteasome subunit beta EC 3.4.25.1 20S proteasome beta subunit Proteasome core protein PrcB |
| Gene Name | prcB SCO1644 SCI41.27 |
| Organism | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces albidoflavus group Streptomyces coelicolor Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Enzyme Sequence | MEANTRSTGRLPAAFLTPGSSSFMDFLGEHQPEMLPGNRQLPPVQGVIEAPHGTTIVAVTFPGGVVLAGDRRATMGNMIAQRDIEKVFPADEYSAVGIAGTAGLAVEMVKLFQLELEHFEKVEGAQLSLEGKANRLSTMIRSNLGMAMQGLAVVPLFAGYDVDRGRGRIFSYDVTGGRSEERHFATTGSGSVFARGAMKKLFRDDLTEEQATTLVVQALYDAADDDSATGGPDVARRIYPIITVITEDGFRRLGEDEAAELAGSVLQARLEQPDGPRAALL |
| Enzyme Length | 281 |
| Uniprot Accession Number | Q7AKQ5 |
| Absorption | |
| Active Site | ACT_SITE 54; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_02113 |
| Activity Regulation | ACTIVITY REGULATION: The formation of the proteasomal ATPase ARC-20S proteasome complex, likely via the docking of the C-termini of ARC into the intersubunit pockets in the alpha-rings, may trigger opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity (By similarity). Peptidolytic activity is completely inhibited by lactacystin, and to a lesser extent, by N-acetyl-Leu-Leu-norleucinal (Ac-LLnL) and benzoyloxycarbonyl-Leu-Leu-Leu-vinylsulfone (Z-LLL-VS) in vitro. {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:9765579}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; Evidence={ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:9765579}; |
| DNA Binding | |
| EC Number | 3.4.25.1 |
| Enzyme Function | FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The S.coelicolor proteasome is able to cleave oligopeptides after hydrophobic residues, but not after basic or acidic residues, thus displaying chymotrypsin-like activity but not trypsin-like activity. {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:9765579}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:9765579}; |
| PH Dependency | |
| Pathway | PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. {ECO:0000255|HAMAP-Rule:MF_02113}. |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Propeptide (1) |
| Keywords | Autocatalytic cleavage;Cytoplasm;Direct protein sequencing;Hydrolase;Protease;Proteasome;Reference proteome;Threonine protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,086 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |