Detail Information for IndEnz0002017380
IED ID IndEnz0002017380
Enzyme Type ID protease017380
Protein Name ATP-dependent Clp protease proteolytic subunit 2
EC 3.4.21.92
Endopeptidase Clp 2
Gene Name clpP2 GOX1520
Organism Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rhodospirillales Acetobacteraceae Gluconobacter Gluconobacter oxydans (Gluconobacter suboxydans) Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Enzyme Sequence MHAGSGNDMDITRMTPTRLDDEPDAPEPETREDDNKTLNSPISELEGRLFDQRKVLIFGGINDKIARDVTGRLLALAGTSDKPIDVYVNSPGGHVESGDTIHDMIRFVDSIAPINMIGTGWVASAGALIYAAGRPERRVCLPNTRFLLHQPMGGVRGPATDIDIEAREIIKMRERLNRIFAKETGQTYEKVAKDTDRNYWMSANEAIAYGLVNRIIHSATELK
Enzyme Length 223
Uniprot Accession Number Q5FQT4
Absorption
Active Site ACT_SITE 124; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_00444; ACT_SITE 149; /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); Compositional bias (1); Region (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 24,703
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda