| IED ID | IndEnz0002004715 |
| Enzyme Type ID | protease004715 |
| Protein Name |
D-gamma-glutamyl-meso-diaminopimelic acid endopeptidase CwlS EC 3.4.19.11 Cell wall lytic enzyme associated with cell separation |
| Gene Name | cwlS yojL BSU19410 |
| 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 | MKKKIVAGLAVSAVVGSSMAAAPAEAKTIKVKSGDSLWKLSRQYDTTISALKSENKLKSTVLYVGQSLKVPESSKKSTTSPSNSSKTSTYTVAYGDSLWMIAKNHKMSVSELKSLNSLSSDLIRPGQKLKIKGTSSSSGSNGSKKNSGSNSSGSSKSTYTVKLGDSLWKIANSLNMTVAELKTLNGLTSDTLYPKQVLKIKGSSSPKNGNSGSKKPSNSNPSKTTTYKVKAGDSLWKIANRLGVTVQSIRDKNNLSSDVLQIGQVLTISGASKSNPSNPTKPTKPKDNSGSNIQIGSKIDRMITEAKKYVGVPYRWGGNTPAGFDCSGFIYYLINNVSSISRLSTAGYWNVMQKVSQPSVGDFVFFTTYKSGPSHMGIYLGGGDFIHASSSGVDISNLSNSYWKQRYLGARSYF |
| Enzyme Length | 414 |
| Uniprot Accession Number | O31852 |
| Absorption | |
| Active Site | ACT_SITE 326; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 375; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 387; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284 |
| Activity Regulation | |
| Binding Site | |
| 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: Probably functions as a cell separation enzyme in addition to LytE and LytF. {ECO:0000269|PubMed:16855244}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 48 degrees Celsius in 50 mM MOPS-NaOH buffer (pH 7.0) without NaCl. {ECO:0000269|PubMed:16855244}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7 without NaCl at 37 degrees Celsius. {ECO:0000269|PubMed:16855244}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (1); Domain (5); Region (3); Signal peptide (1) |
| Keywords | Cell wall biogenesis/degradation;Hydrolase;Protease;Reference proteome;Repeat;Signal;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:16855244}. Note=Localized at cell separation sites and cell poles during late vegetative phase. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,235 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |