IED ID | IndEnz0002010585 |
Enzyme Type ID | protease010585 |
Protein Name |
Gamma-DL-glutamyl hydrolase EC 3.4.19.- Poly-gamma-glutamate depolymerase PGA depolymerase |
Gene Name | pgdS ywtD BSU35860 |
Organism | Bacillus subtilis (strain 168) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
Enzyme Sequence | MNTLANWKKFLLVAVIICFLVPIMTKAEIAEADTSSELIVSEAKNLLGYQYKYGGETPKEGFDPSGLIQYVFSKADIHLPRSVNDQYKIGTAVKPENLKPGDILFFKKEGSTGTVPTHDALYIGDGQMVHSTQSKGVIITNYKKSSYWSGTYIGARRIAADPATADVPVVQEAEKYIGVPYVFGGSTPSEGFDCSGLVQYVFQQALGIYLPRSAEQQWAVGEKVAPQNIKPGDVVYFSNTYKTGISHAGIYAGAGRFIQASRSEKVTISYLSEDYWKSKMTGIRRFDNLTIPKENPIVSEATLYVGEVPYKQGGVTPETGFDTAGFVQYVYQKAAGISLPRYATSQYNAGTKIEKADLKPGDIVFFQSTSLNPSIYIGNGQVVHVTLSNGVTITNMNTSTYWKDKYAGSIRVQ |
Enzyme Length | 413 |
Uniprot Accession Number | P96740 |
Absorption | |
Active Site | ACT_SITE 194; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 247; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 259; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by pretreatment with 1 mM 4-(hydroxymercuri)benzoate, a sulfhydryl inhibitor. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.19.- |
Enzyme Function | FUNCTION: Cleaves, in an endo-type manner, the gamma-glutamyl bond between D-glutamate and L-glutamate of poly-gamma-glutamate (PGA). |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius.; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0.; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Domain (3); Natural variant (3); Signal peptide (1) |
Keywords | Cell wall;Direct protein sequencing;Hydrolase;Protease;Reference proteome;Secreted;Signal;Thiol protease |
Interact With | |
Induction | INDUCTION: In stationary phase; under control of SigD. {ECO:0000269|PubMed:11987133}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. Secreted, cell wall. Note=Cell wall localization shown in PubMed:11987133. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000269|PubMed:10658653 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 45,247 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |