| IED ID | IndEnz0002004004 |
| Enzyme Type ID | protease004004 |
| Protein Name |
ATP-dependent protease ATPase subunit HslU2 Mitochondrial proteasome-like protease HslVU ATPase subunit 2 |
| Gene Name | HslU2 Tb11.01.4050 |
| Organism | Trypanosoma brucei brucei (strain 927/4 GUTat10.1) |
| Taxonomic Lineage | cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Trypanosoma Trypanozoon Trypanosoma brucei Trypanosoma brucei brucei Trypanosoma brucei brucei (strain 927/4 GUTat10.1) |
| Enzyme Sequence | MIRFSWVRLCSSAMAAAAASPDVQAITRAQAMQLDDLSPRKIASILDSYIVGQAEGKRAVAISLRNRWRRRQIEDEGLRRDILPKNILLVGPTGVGKTEISRRMAKLTEAPFVKVEATKYTEVGFKGKDVESIIEDLYSNAKTKAKRRLEIEREKEAHELALEIVFNGWHSCRSASGSFGSSTRNSGSGDSSAEEDKNSSSRDNVTFEEFKEKYKTQFKDDMVVIDVTQQPKGNTKPNASINSVEMLSVGILLGLGSESRGVKTRVTKRVEEALPLATQEALSRLVDETQISALARTLAEQDGVVFIDEIDKVVTEPASANADVSSTGVQQDLLPLIEGSNVTLKDGSQISTDNILFICSGAFHTVKTSDMIAELQGRLPVRVEMHALKEEDIRRILCEPKFNLLLQQKALMKTENIDLEFTPDAVDELARVTTKVNANAQNIGARRLHTVVERVMDEYSFNCQDYEGKKVVIDAEVVRKATGSLMNNIDLAKYIL |
| Enzyme Length | 496 |
| Uniprot Accession Number | Q382V8 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 51; /note=ATP; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250; BINDING 308; /note=ATP; /evidence=ECO:0000250; BINDING 374; /note=ATP; /evidence=ECO:0000250; BINDING 446; /note=ATP; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis (By similarity). The HslVU protease complex functions in mitochondrial DNA replication by regulating DNA helicase PIF2 protein levels. {ECO:0000250, ECO:0000269|PubMed:18421378}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 94..99; /note=ATP; /evidence=ECO:0000250 |
| Features | Binding site (4); Chain (1); Compositional bias (1); Nucleotide binding (1); Region (1); Transit peptide (1) |
| Keywords | ATP-binding;Chaperone;Kinetoplast;Mitochondrion;Nucleotide-binding;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix, kinetoplast {ECO:0000269|PubMed:18421378}. Note=Associated with kinetoplast DNA (kDNA). |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 54,897 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.25.2; |