Detail Information for IndEnz0002011755
IED ID IndEnz0002011755
Enzyme Type ID protease011755
Protein Name Alpha-lytic protease
EC 3.4.21.12
Alpha-lytic endopeptidase
Gene Name alpha-LP
Organism Lysobacter enzymogenes
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Lysobacter Lysobacter enzymogenes
Enzyme Sequence MYVSNHRSRRVARVSVSCLVAALAAMSCGAALAADQVDPQLKFAMQRDLGIFPTQLPQYLQTEKLARTQAAAIEREFGAQFAGSWIERNEDGSFKLVAATSGARKSSTLGGVEVRNVRYSLKQLQSAMEQLDAGANARVKGVSKPLDGVQSWYVDPRSNAVVVKVDDGATEAGVDFVALSGADSAQVRIESSPGKLQTTANIVGGIEYSINNASLCSVGFSVTRGATKGFVTAGHCGTVNATARIGGAVVGTFAARVFPGNDRAWVSLTSAQTLLPRVANGSSFVTVRGSTEAAVGAAVCRSGRTTGYQCGTITAKNVTANYAEGAVRGLTQGNACMGRGDSGGSWITSAGQAQGVMSGGNVQSNGNNCGIPASQRSSLFERLQPILSQYGLSLVTG
Enzyme Length 397
Uniprot Accession Number P00778
Absorption
Active Site ACT_SITE 235; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 262; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 342; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins.; EC=3.4.21.12;
DNA Binding
EC Number 3.4.21.12
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (26); Chain (1); Disulfide bond (3); Helix (10); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (3)
Keywords 3D-structure;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Serine protease;Signal;Zymogen
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000255
Structure 3D NMR spectroscopy (1); X-ray crystallography (48)
Cross Reference PDB 1BOQ; 1GBA; 1GBB; 1GBC; 1GBD; 1GBE; 1GBF; 1GBH; 1GBI; 1GBJ; 1GBK; 1GBL; 1GBM; 1P01; 1P02; 1P03; 1P04; 1P05; 1P06; 1P09; 1P10; 1P11; 1P12; 1QQ4; 1QRW; 1QRX; 1SSX; 1TAL; 2ALP; 2H5C; 2H5D; 2LPR; 2PRO; 2ULL; 3LPR; 3M7T; 3M7U; 3PRO; 3QGJ; 3URC; 3URD; 3URE; 4PRO; 5LPR; 5WOT; 6LPR; 7LPR; 8LPR; 9LPR;
Mapped Pubmed ID 15111063; 16834383; 1931963; 1998685; 22635267; 2611204; 2716847; 29374165; 3122831; 7500345; 9232638;
Motif
Gene Encoded By
Mass 41,077
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.12;