Detail Information for IndEnz0002006050
IED ID IndEnz0002006050
Enzyme Type ID protease006050
Protein Name Gamma-D-glutamyl-L-diamino acid endopeptidase 1
EC 3.4.19.11
Endopeptidase I
Gamma-D-glutamyl-L-diamino acid endopeptidase I
Gamma-D-glutamyl-meso-diaminopimelate peptidase I
Gene Name
Organism Lysinibacillus sphaericus (Bacillus sphaericus)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Lysinibacillus Lysinibacillus sphaericus (Bacillus sphaericus)
Enzyme Sequence MDILIRPGDSLWYFSDLFKIPLQLLLDSNRNINPQLLQVGQRIQIPGYVTTSYTITQGDSLWQIAQNKNLPLNAILLVNPEIQPSRLHIGQTIQVPQRLTWRLVNGQQNYDYSMMMNDIKKLQTAYPFLQGTPIGNSVLAQPIPEILIGNGSKRIHYKASFHANEWITTPIIMTFLNDYLLALTNQTTIRGLSMGPLYNQTTLSLVPMVNPDGVNLVINGPPANEALKNKLIAWNHNSQNFSGWKANINGVDLNDQFPAKWELENARNPQTPGPRDYGGEAPLTQPEAIAMADLTRSRNFAWVLAFHTQGRVIYWGFENLEPPESQTMVEEFSRVSGYEPIQSANSYAGYKDWFIQDWRRPGFTVELGSGTNPLPISEFDTIYQEALGIFLAGLYL
Enzyme Length 396
Uniprot Accession Number Q03415
Absorption
Active Site ACT_SITE 347; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 366; /note=Nucleophile; /evidence=ECO:0000250
Activity Regulation
Binding Site BINDING 255; /note=Substrate; /evidence=ECO:0000250
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of gamma-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A(2)pm) in 7-(L-Ala-gamma-D-Glu)-meso-A(2)pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A(2)pm. It is required that the D-terminal amino and carboxy groups of meso-A(2)pm are unsubstituted.; EC=3.4.19.11;
DNA Binding
EC Number 3.4.19.11
Enzyme Function FUNCTION: An endopeptidase which hydrolyzes the gamma-D-Glu-(L)meso-diaminopimelic acid bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala peptides. It is active on spore cortex peptidoglycan.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Binding site (1); Chain (1); Domain (2); Metal binding (3); Region (1)
Keywords Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Sporulation;Zinc
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 44,724
Kinetics
Metal Binding METAL 162; /note=Zinc; /evidence=ECO:0000250; METAL 165; /note=Zinc; /evidence=ECO:0000250; METAL 307; /note=Zinc; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda