C0MCV8
Gene name |
ddl |
Protein name |
D-alanine--D-alanine ligase |
Names |
D-Ala-D-Ala ligase, D-alanylalanine synthetase |
Species |
Streptococcus equi subsp zooepidemicus (strain H70) |
KEGG Pathway |
seq:SZO_13560 |
EC number |
6.3.2.4: Acid--amino-acid ligases (peptide synthases) |
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 C0MCV8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C0MCV8-F1 | Predicted | AlphaFoldDB |
No variants for C0MCV8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C0MCV8 | |||||
No associated diseases with C0MCV8
5 regional properties for C0MCV8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | D-alanine--D-alanine ligase/VANA/B/C, conserved site | 94 - 105 | IPR000291-1 |
| conserved_site | D-alanine--D-alanine ligase/VANA/B/C, conserved site | 279 - 307 | IPR000291-2 |
| domain | D-alanine--D-alanine ligase, C-terminal | 135 - 333 | IPR011095 |
| domain | D-alanine--D-alanine ligase, N-terminal domain | 6 - 116 | IPR011127 |
| domain | ATP-grasp fold | 132 - 334 | IPR011761 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.2.4 | Acid--amino-acid ligases (peptide synthases) |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| D-alanine-D-alanine ligase activity | Catalysis of the reaction: 2 D-alanine + ATP = D-alanyl-D-alanine + ADP + 2 H(+) + phosphate. |
| metal ion binding | Binding to a metal ion. |
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. |
| peptidoglycan biosynthetic process | The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSKQTLILLY | GGRSAEREVS | VLSAESVMRA | VDYTKFFVKT | YFISQTGQFI | KTQEFSSRPT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LTERLMTNDT | IRLEQQIRPS | DIYEEGAVVF | PVLHGPMGED | GSIQGFLEVL | RMPYVGTNIL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SSSVAMDKIT | TKRVLESAGI | PQVAYTVYIE | GQDLDRCLAE | TEAALSYPVF | VKPANMGSSV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GISKAESEEE | LRAAILLALT | YDSRILIEQG | VLAREIEVGL | LGNTDVKSTL | PGEVVKNVDF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YDYQAKYIDN | EITMAIPATI | DESAMTSMRI | YAETAFKAIG | ACGLSRCDFF | LGQDGQIYLN |
| 310 | 320 | 330 | 340 | ||
| ELNTMPGFTQ | WSMYPLLWEH | MGLNYAELIE | ELVRLAQEMF | EKREGHLI |