| IED ID | IndEnz0002011647 |
| Enzyme Type ID | protease011647 |
| Protein Name |
Proteasome subunit alpha 20S proteasome alpha subunit Proteasome core protein PrcA |
| Gene Name | prcA MSMEG_3894 MSMEI_3804 |
| 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 | MSFPYFISPEQAMRERSELARKGIARGRSVVALAYSEGVLFVAENPSRSLQKVSELYDRVGFAAVGRFNEFDNLRRGGIQFADTRGYAYDRRDVTGRQLANVYAQTLGTIFTEQAKPYEVELCVAEVAHYGETKAPELYRITYDGSIADEPHFVVMGGTTEPIIAALNESYTENASLQDAVEIAVKALSASAEGAEPRSLGPSTLEVAILDAGRPRRAFRRITGAALEALLPEQPQQADSGDKPTE |
| Enzyme Length | 246 |
| Uniprot Accession Number | A0QZ46 |
| Absorption | |
| Active Site | |
| 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_00289, ECO:0000269|PubMed:24986881, ECO:0000269|PubMed:9282749}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| 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). 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_00289, 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_00289}. |
| nucleotide Binding | |
| Features | Chain (1) |
| Keywords | Cytoplasm;Proteasome;Reference proteome;Ubl conjugation |
| Interact With | |
| Induction | INDUCTION: Up-regulated under nitrogen starvation (at protein level). {ECO:0000269|PubMed:24986881}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}. |
| Modified Residue | |
| Post Translational Modification | PTM: Pupylated at an undetermined lysine residue by the prokaryotic ubiquitin-like protein Pup with the help of the ligase PafA, which leads to its degradation by the proteasome and thereby constitutes a negative auto-regulation. {ECO:0000269|PubMed:24986881}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,915 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |