Detail Information for IndEnz0002016825
IED ID IndEnz0002016825
Enzyme Type ID protease016825
Protein Name ATP-dependent Clp protease proteolytic subunit
EC 3.4.21.92
Endopeptidase Clp
Gene Name clpP Smlt0989
Organism Stenotrophomonas maltophilia (strain K279a)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Stenotrophomonas Stenotrophomonas maltophilia group Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia) Stenotrophomonas maltophilia (strain K279a)
Enzyme Sequence MDNRTKALNLVPMVVEQTSRGERAYDIYSRLLKERLIFLVGPIDDHMANVVVAQLLFLESENPEKDINIYINSPGGVVTAGMAIYDTMQYIKPNVSTTCIGQAASMGALLLAAGEAGKRYALPNSRVMIHQPLGGYQGQATDIDIHAREILTLRSRLNEVLAKHTGQSLETIARDTERDNFKSAFEAQAYGLVDQVLERRPDESIQAG
Enzyme Length 208
Uniprot Accession Number B2FQR2
Absorption
Active Site ACT_SITE 105; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_00444; ACT_SITE 130; /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 22,962
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda