| IED ID | IndEnz0002010969 |
| Enzyme Type ID | protease010969 |
| Protein Name |
Gamma-D-glutamyl-L-lysine dipeptidyl-peptidase EC 3.4.14.13 Gamma-D-glutamyl-L-diamino acid endopeptidase |
| Gene Name | ykfC BCE_2878 |
| Organism | Bacillus cereus (strain ATCC 10987 / NRS 248) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus cereus group Bacillus cereus Bacillus cereus (strain ATCC 10987 / NRS 248) |
| Enzyme Sequence | MKKVGTAFLTTLFIFSSFTSAHAEEKKDSKAFIDVSAATLWTAPDSLRPIDVPSATNPVDLWKWTKSMTLDEKLWLTNANKLETQALLGQEVTVVDKKGDWVKVLVHGQPTPRNEEGYPGWMPEKQLTYNQEFADKTNEPFVLVTKPTAILYINPSEKHKSLEVSYNTRLPLLSEDTISYRVLLPNGQKAWLRKNDGTFYRSQNDIPTPAADDLINTGKMFLGLPYIWAGTSGFGFDCSGFTHTIYKSHGITIPRDSGPQSRNGVAVDKEHLQKGDLIFFAHDQGKGSVHHVAMYIGDGNMIHSPRAERSVEIIPLNTPGYIEEYAGARRYLP |
| Enzyme Length | 333 |
| Uniprot Accession Number | Q736M3 |
| Absorption | |
| Active Site | ACT_SITE 238; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01284, ECO:0000305|PubMed:20944232"; ACT_SITE 291; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01284, ECO:0000305|PubMed:20944232"; ACT_SITE 303; /evidence="ECO:0000255|PROSITE-ProRule:PRU01284, ECO:0000305|PubMed:20944232" |
| Activity Regulation | |
| Binding Site | BINDING 83; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:20944232; BINDING 118; /note=Substrate; /evidence=ECO:0000269|PubMed:20944232 |
| 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:0000250|UniProtKB:O35010}; |
| 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:0000250|UniProtKB:O35010}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall degradation; peptidoglycan degradation. {ECO:0000250|UniProtKB:O35010}. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (21); Binding site (2); Chain (1); Domain (1); Helix (14); Region (2); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Cell wall biogenesis/degradation;Hydrolase;Protease;Signal;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3H41; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 37,274 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.13; |