Detail Information for IndEnz0002007078
IED ID IndEnz0002007078
Enzyme Type ID protease007078
Protein Name Protease 2
EC 3.4.21.83
Oligopeptidase B
Protease II
Gene Name ptrB tlp b1845 JW1834
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MLPKAARIPHAMTLHGDTRIDNYYWLRDDTRSQPEVLDYLQQENSYGHRVMASQQALQDRILKEIIDRIPQREVSAPYIKNGYRYRHIYEPGCEYAIYQRQSAFSEEWDEWETLLDANKRAAHSEFYSMGGMAITPDNTIMALAEDFLSRRQYGIRFRNLETGNWYPELLDNVEPSFVWANDSWIFYYVRKHPVTLLPYQVWRHAIGTPASQDKLIYEEKDDTYYVSLHKTTSKHYVVIHLASATTSEVRLLDAEMADAEPFVFLPRRKDHEYSLDHYQHRFYLRSNRHGKNFGLYRTRMRDEQQWEELIPPRENIMLEGFTLFTDWLVVEERQRGLTSLRQINRKTREVIGIAFDDPAYVTWIAYNPEPETARLRYGYSSMTTPDTLFELDMDTGERRVLKQTEVPGFYAANYRSEHLWIVARDGVEVPVSLVYHRKHFRKGHNPLLVYGYGSYGASIDADFSFSRLSLLDRGFVYAIVHVRGGGELGQQWYEDGKFLKKKNTFNDYLDACDALLKLGYGSPSLCYAMGGSAGGMLMGVAINQRPELFHGVIAQVPFVDVVTTMLDESIPLTTGEFEEWGNPQDPQYYEYMKSYSPYDNVTAQAYPHLLVTTGLHDSQVQYWEPAKWVAKLRELKTDDHLLLLCTDMDSGHGGKSGRFKSYEGVAMEYAFLVALAQGTLPATPAD
Enzyme Length 686
Uniprot Accession Number P24555
Absorption
Active Site ACT_SITE 532; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:1769955"; ACT_SITE 617; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"; ACT_SITE 652; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of -Arg-|-Xaa- and -Lys-|-Xaa- bonds in oligopeptides, even when P1' residue is proline.; EC=3.4.21.83;
DNA Binding
EC Number 3.4.21.83
Enzyme Function FUNCTION: Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Sequence conflict (1)
Keywords Direct protein sequencing;Hydrolase;Protease;Reference proteome;Serine protease
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 1447164; 15948139; 16606699; 7845209; 9533626;
Motif
Gene Encoded By
Mass 79,491
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.83;