Detail Information for IndEnz0002011648
IED ID IndEnz0002011648
Enzyme Type ID protease011648
Protein Name Proteasome subunit beta 2
EC 3.4.25.1
20S proteasome beta subunit 2
Proteasome core protein PsmB 2
Gene Name psmB2 Kcr_1461
Organism Korarchaeum cryptofilum (strain OPF8)
Taxonomic Lineage cellular organisms Archaea TACK group Candidatus Korarchaeota Candidatus Korarchaeum Candidatus Korarchaeum cryptofilum Korarchaeum cryptofilum (strain OPF8)
Enzyme Sequence MVLATALGLRFDGGVVLAADRRVSYNGFILSKSARKVFLINERVGVSTAGLPGDFQELVDVLKYNITMYELENEKAATPTNVAKLLSILLYQGRFSGIYYAELVVGGIDNSGPKIFVLDPAGGLMEENFSAVGSGAQIATGILERFFKEGMSEKEAVELAERAMREAISRDALSGDGIDLLIITSKGSRMEFIPVRTA
Enzyme Length 198
Uniprot Accession Number B1L6X8
Absorption
Active Site ACT_SITE 5; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_02113
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}.
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};
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. {ECO:0000255|HAMAP-Rule:MF_02113}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Propeptide (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 21,362
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda