Detail Information for IndEnz0002018022
IED ID IndEnz0002018022
Enzyme Type ID protease018022
Protein Name ATP-dependent Clp protease proteolytic subunit
EC 3.4.21.92
Endopeptidase Clp
Gene Name clpP llmg_0638
Organism Lactococcus lactis subsp. cremoris (strain MG1363)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Lactococcus (lactic streptococci) Lactococcus lactis subsp. cremoris (Streptococcus cremoris) Lactococcus cremoris subsp. cremoris Lactococcus lactis subsp. cremoris (strain MG1363)
Enzyme Sequence MGYLVPTVIEQSSRGERAYDIYSRLLKDRIIMLTGPVEDGMANSIIAQLLFLDAQDNTKDIYLYVNTPGGSVSAGLAIVDTMNFIKSDVQTIVMGMAASMGTIIASSGTKGKRFMLPNAEYLIHQPMGGAGQGTQQTDMAIVAEQLLKTRKRLEQILADNSNRSLEQIHKDAERDHWMDAKETLEYGFIDEIMENNSLK
Enzyme Length 199
Uniprot Accession Number Q9ZAB0
Absorption
Active Site ACT_SITE 99; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_00444; ACT_SITE 124; /evidence=ECO:0000255|HAMAP-Rule:MF_00444
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).; EC=3.4.21.92; Evidence={ECO:0000255|HAMAP-Rule:MF_00444};
DNA Binding
EC Number 3.4.21.92
Enzyme Function FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. {ECO:0000255|HAMAP-Rule:MF_00444}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1)
Keywords Cytoplasm;Hydrolase;Protease;Serine protease;Stress response
Interact With
Induction INDUCTION: By heat shock.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 22,052
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.92;