IED ID | IndEnz0002001621 |
Enzyme Type ID | protease001621 |
Protein Name |
Proteasome subunit beta EC 3.4.25.1 20S proteasome beta subunit Proteasome core protein PrcB |
Gene Name | prcB MSMEG_3895 MSMEI_3805 |
Organism | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycolicibacterium Mycolicibacterium smegmatis (Mycobacterium smegmatis) Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
Enzyme Sequence | MTWRDNQSFPQPTLNTTGIPSVPVDLSSFSELLSRQAPELLPVNRVAYGTTPVGPTDAVPHGTTIVALKYPGGVLIAGDRRSTQGNMIAGRDVQKVYITDDYTATGIAGTAAIAVEFARLYAVELEHYEKLEGVPLTFRGKVNRLAIMVRGNLGAALQGFVALPLLVGYDLDDPHPEGAGRIVSFDAAGGWNIEEEGYQSVGSGSIFAKSSMKKLYSQVSDADSALKVAVEALYDAADDDSATGGPDLVRGIYPTAVTIGAEGAEEVPETRIAELAREVIESRSRTDTFGPDARRGIDARGDS |
Enzyme Length | 303 |
Uniprot Accession Number | A0QZ47 |
Absorption | |
Active Site | ACT_SITE 63; /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). PPS auto-regulates its own activity via pupylation and degradation of its components (PubMed:24986881). Peptidolytic activity is inhibited by N-acetyl-Leu-Leu-norleucinal (Ac-LLnL) in vitro (PubMed:9282749). {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:24986881, ECO:0000269|PubMed:9282749}. |
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:19028679, ECO:0000269|PubMed:9282749}; |
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 M.smegmatis proteasome is able to cleave oligopeptides after hydrophobic residues, thus displaying chymotrypsin-like activity. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.smegmatis proteasome are the pupylated SodA and Ino1 proteins (PubMed:19028679). The Pup-proteasome system (PPS) is essential for survival under starvation; PPS likely functions to recycle amino acids under nitrogen starvation, thereby enabling the cell to maintain basal metabolic activities (PubMed:24986881). {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:19028679, ECO:0000269|PubMed:24986881, ECO:0000269|PubMed:9282749}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. {ECO:0000255|HAMAP-Rule:MF_02113}. |
nucleotide Binding | |
Features | Active site (1); Chain (1); Erroneous initiation (1); Propeptide (1); Region (1) |
Keywords | Autocatalytic cleavage;Cytoplasm;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 | 32,131 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |