Detail Information for IndEnz0002015067
IED ID IndEnz0002015067
Enzyme Type ID protease015067
Protein Name ATP-dependent protease subunit HslV
EC 3.4.25.2
Gene Name hslV BT0296
Organism Borrelia turicatae (strain 91E135)
Taxonomic Lineage cellular organisms Bacteria Spirochaetes Spirochaetia Spirochaetales Borreliaceae Borrelia Borrelia turicatae Borrelia turicatae (strain 91E135)
Enzyme Sequence MSFKGTTVIAIRRGGKTVVAADGQVTFGYTVLKSNAIKIRKLFNGKILAGFAGSTSDAITLFEKFEEKVKAREDGIIDIKRAAVELAKDWRSDKILHKLEAMMLVADSENILLISGTGDVVEPEEDVISIGSGGNYAYSAALAYMENKKLSAADIAFKSLKVAARVCIYTNSNIVLEEIS
Enzyme Length 180
Uniprot Accession Number A1QZ92
Absorption
Active Site ACT_SITE 6; /evidence=ECO:0000255|HAMAP-Rule:MF_00248
Activity Regulation ACTIVITY REGULATION: Allosterically activated by HslU binding. {ECO:0000255|HAMAP-Rule:MF_00248}.
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:0000255|HAMAP-Rule:MF_00248};
DNA Binding
EC Number 3.4.25.2
Enzyme Function FUNCTION: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. {ECO:0000255|HAMAP-Rule:MF_00248}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (3)
Keywords Allosteric enzyme;Cytoplasm;Hydrolase;Metal-binding;Protease;Sodium;Threonine protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00248}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 19,441
Kinetics
Metal Binding METAL 164; /note=Sodium; via carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00248; METAL 167; /note=Sodium; via carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00248; METAL 170; /note=Sodium; via carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00248
Rhea ID
Cross Reference Brenda