Detail Information for IndEnz0002017091
IED ID IndEnz0002017091
Enzyme Type ID protease017091
Protein Name ATP-dependent Clp protease proteolytic subunit 1
EC 3.4.21.92
Endopeptidase Clp 1
Gene Name clpP1 CCA_00225
Organism Chlamydophila caviae (strain ATCC VR-813 / DSM 19441 / GPIC) (Chlamydia caviae)
Taxonomic Lineage cellular organisms Bacteria PVC group Chlamydiae Chlamydiia Chlamydiales Chlamydiaceae Chlamydia/Chlamydophila group Chlamydia Chlamydia caviae (Chlamydophila caviae) Chlamydophila caviae (strain ATCC VR-813 / DSM 19441 / GPIC) (Chlamydia caviae)
Enzyme Sequence MPDGEVNKLRDVIDKKILDARRVFFSEPVTDKSAADAIKKLWYLELSHPGQPIVFVINSPGGSVDAGFAVWDQIKMMTSPVTTVVTGLAASMGSVLSLCAAPGRRFATPHSRIMIHQPSIGGPITGQATDLDIHAREILKTKKRIVDVYLEATGQPREVIEKAIDRDMWMTADEAKDFGLLDGILFSFDDL
Enzyme Length 191
Uniprot Accession Number Q824C7
Absorption
Active Site ACT_SITE 91; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_00444; ACT_SITE 116; /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 20,951
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda