| IED ID | IndEnz0002008700 |
| Enzyme Type ID | protease008700 |
| Protein Name |
Proteasome subunit beta EC 3.4.25.1 20S proteasome beta subunit Proteasome core protein PsmB |
| Gene Name | psmB Ta0612 |
| Organism | Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) |
| Taxonomic Lineage | cellular organisms Archaea Candidatus Thermoplasmatota Thermoplasmata Thermoplasmatales Thermoplasmataceae Thermoplasma Thermoplasma acidophilum Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) |
| Enzyme Sequence | MNQTLETGTTTVGITLKDAVIMATERRVTMENFIMHKNGKKLFQIDTYTGMTIAGLVGDAQVLVRYMKAELELYRLQRRVNMPIEAVATLLSNMLNQVKYMPYMVQLLVGGIDTAPHVFSIDAAGGSVEDIYASTGSGSPFVYGVLESQYSEKMTVDEGVDLVIRAISAAKQRDSASGGMIDVAVITRKDGYVQLPTDQIESRIRKLGLIL |
| Enzyme Length | 211 |
| Uniprot Accession Number | P28061 |
| Absorption | |
| Active Site | ACT_SITE 9; /note="Nucleophile"; /evidence="ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:7725107" |
| Activity Regulation | ACTIVITY REGULATION: The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers 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. {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:17803938, ECO:0000269|PubMed:20360109}. |
| 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:8999862}; |
| 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 T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities. {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:8999862}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Chain (1); Helix (5); Mutagenesis (1); Propeptide (1); Turn (2) |
| Keywords | 3D-structure;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 | Electron microscopy (11); X-ray crystallography (8) |
| Cross Reference PDB | 1PMA; 1YA7; 1YAR; 1YAU; 3C91; 3C92; 3IPM; 3J9I; 3JRM; 3JSE; 3JTL; 5VY3; 5VY4; 6BDF; 6UTF; 6UTG; 6UTH; 6UTI; 6UTJ; |
| Mapped Pubmed ID | 23644547; 25760083; 28991891; 32917864; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,147 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=39 uM for Suc-LLVY-Amc (at 55 degrees Celsius) {ECO:0000269|PubMed:8999862}; Vmax=28 nmol/min/mg enzyme with Suc-LLVY-Amc as substrate (at 55 degrees Celsius) {ECO:0000269|PubMed:8999862}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.25.1; |