IED ID | IndEnz0002002922 |
Enzyme Type ID | protease002922 |
Protein Name |
Leupeptin-inactivating enzyme 2 LIE2 EC 3.4.24.- |
Gene Name | lieB |
Organism | Streptomyces exfoliatus (Streptomyces hydrogenans) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces exfoliatus (Streptomyces hydrogenans) |
Enzyme Sequence | MAAMALTASLAGALAGTASAAQQAQPSPSQKDTPAARAVAAADQAVDSGLDSLVNSSQEQYERRLVTPWVKDLYSVSYERSYRGLPVVGGDAVVLADGTGKVRALQSASSVRIDVSTQASVSAKDAESTSRAKLVSVDKVESSRLVVRLKDDKPVLAWETVLSGRTKTAPSKLHVFVDARTGAFVDSYDEVVAGTGNSKWNGPGPVTIDTTNSGSTYTLRDPVRTGLSCADYSTGTVFSKSSDSWGTGNPTSKETGCVDLMFAAQKQWDMLSQWLGRNGVSGNGRSFPAKVGLSDLNAYWDGSSVTIGRNSAGEWIAGIDVVAHEYGHAIDSNTPGGTSGQESGLGEATGDIFGALTEAFANEPAPYDTPDYTVGEVINLQGRGPIRNMYNPPAVNNDPACYSSAIPGTEVHAAAGPLNHWFYLLAEGTSPGGGKPNSSTCNGTSLTGVGVQNAGKIFYGGMLLKTSSMSYKKYRTATLSSAKSLDATCDLFNKTKAAWDGISVPAQTADPTCTPSGQNNDFSMSLSPSSGTVQQGASVTTTVGTTVTTGNAQSVTLTASGLPAGVSASFNPATVQSGQSSVLTLTATANAAPGASTIVVKGQGASLSHTVDYALNVGGTQPGNDPPDIDVANVQAHLTQFNTIASQNGGHRRAGSAGYTQSLAYVKGKLQAAGYTVTEQNCTSCTYPSNNLIADWPGGPADQTVMFGAHLDGVSAGPGINDNGSGSATLLENALVLAQKNPTMTKHVRFAWWTDEEQGLNGSEFYVNQLSSAQRSAIKGYYNFDMVGSTNGGYFINNVNSTTAAPLKAYWTSLNLAPEENTEGQGRSDDYSFQQAGIPTSGYAAGASARKTSAQATKWGGTANAAYDPCYHSSCDTTNNINATVLNRSADGVAYAVWKQAVGGETPAQDFSVAVSPSAGSAAPGGSTSATVNTATVSGAAQTVALSVSGAPAGVTATLSPTSVQSGSSSALSVQVGASTAPGTYTLTVTGSGTVSHTSTYSLTVTGGGSCTPRQLVTNGGFESGSSPWSATAGQTLETLSNLNANSGYAEKSYDLSQFAGQTVTLKFTGTEDQSLQTSFVVDDVTVQVS |
Enzyme Length | 1090 |
Uniprot Accession Number | P83913 |
Absorption | |
Active Site | ACT_SITE 756; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P80561 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: A leucine-specific metalloprotease that plays a role in controlling the amount of leupeptin during colony development. Degrades leupeptin into three components, acetyl-leucine, leucine and argininal (By similarity). {ECO:0000250|UniProtKB:P81715}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Metal binding (6); Region (2); Signal peptide (1); Site (1) |
Keywords | Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P81715}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 111,736 |
Kinetics | |
Metal Binding | METAL 710; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P81715; METAL 722; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 722; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 757; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 785; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P81715; METAL 872; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561 |
Rhea ID | |
Cross Reference Brenda |