| IED ID | IndEnz0002010774 |
| Enzyme Type ID | protease010774 |
| Protein Name |
Proteasome subunit beta EC 3.4.25.1 20S proteasome beta subunit Proteasome core protein PsmB |
| Gene Name | psmB HVO_1562 |
| Organism | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Stenosarchaea group Halobacteria Haloferacales Haloferacaceae Haloferax Haloferax volcanii (Halobacterium volcanii) Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
| Enzyme Sequence | MRTPTHDEFSGRLDSLNGDRSNVFGPELGEFSNADRRADELGDKETKTGTTTVGIKTEEGVVLATDMRASMGYMVSSKDVQKVEEIHPTGALTIAGSVSAAQSLISSLRAEVRLYEARRGEDMSMQALSTLVGNFLRSGGFYVVQPILGGVDETGPHIYSIDPAGSILEEEYTVTGSGSQYALGVLEQEFEDGLSIEEAKGVATKAIRSAVERDLASGNGINIAVVTEDGVDIQRHQNFEGLE |
| Enzyme Length | 243 |
| Uniprot Accession Number | D4GYZ1 |
| Absorption | |
| Active Site | ACT_SITE 50; /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 (By similarity). In vitro, the chymotrypsin-like activity of the alpha1-beta proteasome is potently inhibited by carbobenzoxyl-leucinyl-leucinyl-leucinal-H (MG132) and significantly by N-acetyl-leucinyl-leucinyl-norleucinal-H (calpain inhibitor I). {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:10482525}. |
| 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:10482525}; |
| 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 H.volcanii alpha1-beta proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activity but no trypsin-like activity. {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:10482525}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype). {ECO:0000269|PubMed:10482525}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-9.3 for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype). {ECO:0000269|PubMed:10482525}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Modified residue (1); Propeptide (1); Region (1) |
| Keywords | Autocatalytic cleavage;Cytoplasm;Direct protein sequencing;Hydrolase;Phosphoprotein;Protease;Proteasome;Reference proteome;Threonine protease;Zymogen |
| Interact With | |
| Induction | INDUCTION: Up-regulated at the mRNA level during transition from exponential to stationary phase. However, at the protein level, PsmB is expressed at a high and relatively constant level throughout growth. {ECO:0000269|PubMed:15516591}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}. |
| Modified Residue | MOD_RES 129; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:16950923 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 25,994 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |