Detail Information for IndEnz0002016847
IED ID IndEnz0002016847
Enzyme Type ID protease016847
Protein Name ATP-dependent Clp protease proteolytic subunit
EC 3.4.21.92
Endopeptidase Clp
Gene Name clpP SZO_03580
Organism Streptococcus equi subsp. zooepidemicus (strain H70)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus dysgalactiae group Streptococcus equi Streptococcus equi subsp. zooepidemicus Streptococcus equi subsp. zooepidemicus (strain H70)
Enzyme Sequence MIPVVIEQTSRGERSYDIYSRLLKDRIIMLTGPVEDNMANSVIAQLLFLDAQDNTKDIYLYVNTPGGSVSAGLAIVDTMNFIKADVQTIVMGMAASMGTVIASSGAKGKRFMLPNAEYMIHQPMGGTGGGTQQTDMAIAAEHLLKTRHRLEKILAQNAGKTIKQIHKDAERDYWMSAEETLAYGFIDEIMENNELA
Enzyme Length 196
Uniprot Accession Number C0MGT5
Absorption
Active Site ACT_SITE 96; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_00444; ACT_SITE 121; /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
Interact With
Induction
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 21,562
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda