Detail Information for IndEnz0002001621
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