Detail Information for IndEnz0002017137
IED ID IndEnz0002017137
Enzyme Type ID protease017137
Protein Name ATP-dependent Clp protease proteolytic subunit 1
EC 3.4.21.92
Endopeptidase Clp 1
Gene Name clpP1 GOX0087
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 MTIRDRDPLEVFSNSLVPMVVEQTARGERSFDIFSRLLQERIIFLTGPVYDQVSSLICAQLLYLESVNPTKEISFYINSPGGVVSAGLAIYDTMQYIRCPVSTVCIGQAASMGSLLLAGGEKGHRYALPNARVMVHQPSGGAQGQASDIEIQAREILIIRQRLNEIYREHTGQTLEQIEQKLERDSYLSANEAREFGLIDKVVERNPHETTPDPS
Enzyme Length 215
Uniprot Accession Number Q5FUR3
Absorption
Active Site ACT_SITE 111; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_00444; ACT_SITE 136; /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 23,969
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda