Detail Information for IndEnz0002018338
IED ID IndEnz0002018338
Enzyme Type ID protease018338
Protein Name ATP-dependent Clp protease proteolytic subunit 2
EC 3.4.21.92
Endopeptidase Clp 2
Gene Name clpP2 clpP-2 TP_1041
Organism Treponema pallidum (strain Nichols)
Taxonomic Lineage cellular organisms Bacteria Spirochaetes Spirochaetia Spirochaetales Treponemataceae Treponema Treponema pallidum Treponema pallidum subsp. pallidum (syphilis treponeme) Treponema pallidum (strain Nichols)
Enzyme Sequence MRCDATQEKRAHSESGESVFFQKFLETRQILLSGEISKDLAEGIVRQLFVLESLSVSKPIYMYVDSPGGDVDAGYAIFDVIRFVKTPVYTIGMGLVASAGVLVLLAAKKDCRFGLRNSRYLIHQPLSGMRGVATDIEIHARELEKTRSKLNALIASETGVSLDKVAQDTNRDYWLDASQALEYGLISNLIEKRADLPKK
Enzyme Length 199
Uniprot Accession Number O84003
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); Erroneous initiation (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 22,086
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.92;