Detail Information for IndEnz0002017298
IED ID IndEnz0002017298
Enzyme Type ID protease017298
Protein Name ATP-dependent Clp protease proteolytic subunit 2
EC 3.4.21.92
Endopeptidase Clp 2
Gene Name clpP2 clpP-2 BB_0757
Organism Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Taxonomic Lineage cellular organisms Bacteria Spirochaetes Spirochaetia Spirochaetales Borreliaceae Borreliella Borrelia burgdorferi (Lyme disease spirochete) (Borreliella burgdorferi) Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Enzyme Sequence MTGKEDNDACVLHDKSLKLVLKSRSIVIAGEITKDVSRLFQEKILLLEALDFKKPIFVYIDSEGGDIDAGFAIFNMIRFVKPKVFTVGVGLVASAAALIFLAAKLENRFSLPFARYLLHQPLSGFKGVATDIEIYTNELNKVKKELNNIISKETGQKISKIEKDTDRDFWLDSSAAKKYGLVFEVVETKYQLEEFISA
Enzyme Length 198
Uniprot Accession Number O51698
Absorption
Active Site ACT_SITE 94; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_00444; ACT_SITE 119; /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;Reference proteome;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 22,216
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.92;