| IED ID | IndEnz0002012094 |
| Enzyme Type ID | protease012094 |
| Protein Name |
Gamma-D-glutamyl-L-lysine dipeptidyl-peptidase EC 3.4.14.13 Cell wall endopeptidase YkfC |
| Gene Name | ykfC BSU12990 |
| 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 | MMHTVISAVANIWTAPDSPRPSDQFMLQPTVMIRDWLERMTYDERLGLCTDNVIQTQVLFGEKVLVTAEQGEWVSVIVPSQPSRKDPRGYPGWMKKYQLEKTKPIHTQHDVMISKPAAFLYRSNGEKEIELSFLTVLPLIAKENGYFKVSTVFGERFVRQSDAVPVSQQKGTAEDIIQTGAFFLGLPYLWGGISGFGFDCSGFMYSIFKANGYSIPRDAGDQAKAGKGVPLDDMKAGDLLFFAYEEGKGAIHHVGLYVGGGKMLHSPKTGKSIEILTLTETIYEKELCAVRRCFSE |
| Enzyme Length | 296 |
| Uniprot Accession Number | O35010 |
| Absorption | |
| Active Site | ACT_SITE 200; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 253; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 265; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284 |
| Activity Regulation | |
| Binding Site | BINDING 90; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q736M3 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=The enzyme releases L-Ala-gamma-D-Glu dipeptides from cell wall peptides via cleavage of an L-Ala-gamma-D-Glu-|-L-Lys bond.; EC=3.4.14.13; Evidence={ECO:0000269|PubMed:11747447}; |
| DNA Binding | |
| EC Number | 3.4.14.13 |
| Enzyme Function | FUNCTION: Specifically hydrolyzes gamma-D-glutamyl-L-lysine bonds in murein peptides, releasing L-Ala-D-Glu. {ECO:0000269|PubMed:11747447}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall degradation; peptidoglycan degradation. {ECO:0000305|PubMed:11747447}. |
| nucleotide Binding | |
| Features | Active site (3); Binding site (1); Chain (1); Domain (1); Region (2); Sequence conflict (1) |
| Keywords | Cell wall biogenesis/degradation;Hydrolase;Protease;Reference proteome;Thiol protease |
| Interact With | |
| Induction | INDUCTION: Repressed by AbrB, a transcription factor that negatively controls biofilm formation. {ECO:0000269|PubMed:15101989}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,025 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=310 uM for L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala {ECO:0000269|PubMed:11747447}; KM=120 uM for L-Ala-gamma-D-Glu-L-Lys-D-Ala {ECO:0000269|PubMed:11747447}; KM=290 uM for L-Ala-gamma-D-Glu-L-Lys {ECO:0000269|PubMed:11747447}; Note=kcat is 5.7 sec(-1) with L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala as substrate. kcat is 2.6 sec(-1) with L-Ala-gamma-D-Glu-L-Lys-D-Ala as substrate. kcat is 1.2 sec(-1) with L-Ala-gamma-D-Glu-L-Lys as substrate. {ECO:0000269|PubMed:11747447}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.13; |