Detail Information for IndEnz0002002922
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