Q03415
Gene name |
|
Protein name |
Gamma-D-glutamyl-L-diamino acid endopeptidase 1 |
Names |
Endopeptidase I, Gamma-D-glutamyl-L-diamino acid endopeptidase I, Gamma-D-glutamyl-meso-diaminopimelate peptidase I |
Species |
Lysinibacillus sphaericus (Bacillus sphaericus) |
KEGG Pathway |
ag:CAA49259 |
EC number |
3.4.19.11: Omega peptidases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q03415
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q03415-F1 | Predicted | AlphaFoldDB |
No variants for Q03415
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q03415 | |||||
No associated diseases with Q03415
4 regional properties for Q03415
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M14, carboxypeptidase A | 109 - 385 | IPR000834 |
| domain | LysM domain | 1 - 46 | IPR018392-1 |
| domain | LysM domain | 51 - 96 | IPR018392-2 |
| domain | ENP1, carboxypeptidase domain | 155 - 390 | IPR034274 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.19.11 | Omega peptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metallocarboxypeptidase activity | Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
| zinc ion binding | Binding to a zinc ion (Zn). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cell wall organization | A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| sporulation resulting in formation of a cellular spore | The process in which a relatively unspecialized cell acquires the specialized features of a cellular spore, a cell form that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDILIRPGDS | LWYFSDLFKI | PLQLLLDSNR | NINPQLLQVG | QRIQIPGYVT | TSYTITQGDS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LWQIAQNKNL | PLNAILLVNP | EIQPSRLHIG | QTIQVPQRLT | WRLVNGQQNY | DYSMMMNDIK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KLQTAYPFLQ | GTPIGNSVLA | QPIPEILIGN | GSKRIHYKAS | FHANEWITTP | IIMTFLNDYL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LALTNQTTIR | GLSMGPLYNQ | TTLSLVPMVN | PDGVNLVING | PPANEALKNK | LIAWNHNSQN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FSGWKANING | VDLNDQFPAK | WELENARNPQ | TPGPRDYGGE | APLTQPEAIA | MADLTRSRNF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AWVLAFHTQG | RVIYWGFENL | EPPESQTMVE | EFSRVSGYEP | IQSANSYAGY | KDWFIQDWRR |
| 370 | 380 | 390 | |||
| PGFTVELGSG | TNPLPISEFD | TIYQEALGIF | LAGLYL |