Detail Information for IndEnz0002015131
IED ID IndEnz0002015131
Enzyme Type ID protease015131
Protein Name ATP-dependent protease subunit HslV
EC 3.4.25.2
Gene Name hslV clpQ SA1096
Organism Staphylococcus aureus (strain N315)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain N315)
Enzyme Sequence MSNTTLHATTIYAVRHNGKAAMAGDGQVTLGQQVIMKQTARKVRRLYEGKVLAGFAGSVADAFTLFEKFETKLQQFSGNLERAAVELAQEWRGDKQLRQLEAMLIVMDKDAILVVSGTGEVIAPDDDLIAIGSGGNYALSAGRALKRHASHLSAEEMAYESLKVAADICVFTNDNIVVETL
Enzyme Length 181
Uniprot Accession Number P65797
Absorption
Active Site ACT_SITE 9; /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 19,572
Kinetics
Metal Binding METAL 166; /note=Sodium; via carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00248; METAL 169; /note=Sodium; via carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00248; METAL 172; /note=Sodium; via carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00248
Rhea ID
Cross Reference Brenda