Detail Information for IndEnz0002015196
IED ID IndEnz0002015196
Enzyme Type ID protease015196
Protein Name ATP-dependent protease subunit HslV
EC 3.4.25.2
Mitochondrial proteasome-like protease HslVU protease subunit
Gene Name HslV Tb11.01.2000
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 MLRRVGRTTCSPAACQLRHTTILSVRKGDTVVLLGDRQVTLGERIVAKSSACKLRRINDDVVIGFAGSTADAISLMEKLENKIGEFPNQLTRAAVELAKEWRTDRALRRLEASLIVCSAEETLEIDGQGNVITPEADGIVAIGSGGTFAKAAARALIDVDGYDAEKIARKAMRIATDIDVFSNEHWDVEVLKRKSEKQEGSEASAKTSE
Enzyme Length 209
Uniprot Accession Number Q383Q5
Absorption
Active Site ACT_SITE 20; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=ATP-dependent cleavage of peptide bonds with broad specificity.; EC=3.4.25.2; Evidence={ECO:0000269|PubMed:18421378};
DNA Binding
EC Number 3.4.25.2
Enzyme Function FUNCTION: Protease subunit of a proteasome-like degradation complex. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins (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
Features Active site (1); Beta strand (10); Chain (1); Helix (5); Mutagenesis (3); Transit peptide (1); Turn (1)
Keywords 3D-structure;Hydrolase;Kinetoplast;Mitochondrion;Protease;Reference proteome;Threonine protease;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 X-ray crystallography (2)
Cross Reference PDB 4HNZ; 4HO7;
Mapped Pubmed ID 23818520;
Motif
Gene Encoded By
Mass 22,684
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.25.2;