Detail Information for IndEnz0002018142
IED ID IndEnz0002018142
Enzyme Type ID protease018142
Protein Name ATP-dependent Clp protease proteolytic subunit
EC 3.4.21.92
Endopeptidase Clp
Gene Name clpP Nther_1102
Organism Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Natranaerobiales Natranaerobiaceae Natranaerobius Natranaerobius thermophilus Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF)
Enzyme Sequence MNLIPMVIEQTNRGERSYDIYSRLLKDRIIFIGTGINDDIANSVIAQMLFLESEDPDKDIHLYINSPGGHVHAGLAIYDTMQYIRSDVSTICVGMAASMGAVLLAAGNEGKRFCLPNSRIMLHQPMGGAQGQAADVEIHAREIMKTKERLNQILAHHTGQPVEQISKDTDRDFFMSSEEAQKYGVIDDVLKRPPENS
Enzyme Length 197
Uniprot Accession Number B2A158
Absorption
Active Site ACT_SITE 98; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_00444; ACT_SITE 123; /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 21,916
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda