C5D5L4
Gene name |
clpX |
Protein name |
ATP-dependent Clp protease ATP-binding subunit ClpX |
Names |
|
Species |
Geobacillus sp (strain WCH70) |
KEGG Pathway |
gwc:GWCH70_2587 |
EC number |
|
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 C5D5L4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C5D5L4-F1 | Predicted | AlphaFoldDB |
No variants for C5D5L4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C5D5L4 | |||||
No associated diseases with C5D5L4
5 regional properties for C5D5L4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phospholipase D/Transphosphatidylase | 219 - 246 | IPR001736-1 |
| domain | Phospholipase D/Transphosphatidylase | 399 - 426 | IPR001736-2 |
| domain | Phospholipase D-like domain | 135 - 248 | IPR025202-1 |
| domain | Phospholipase D-like domain | 326 - 445 | IPR025202-2 |
| domain | Cardiolipin synthase N-terminal | 22 - 59 | IPR027379 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| protein dimerization activity | The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. |
| unfolded protein binding | Binding to an unfolded protein. |
| zinc ion binding | Binding to a zinc ion (Zn). |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFKFNDEKGQ | LKCSFCGKTQ | DQVRKLVAGP | GVYICDECIE | LCTEIVEEEL | GNEEEFEFKD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IPKPKEIREI | LDEYVIGQDE | AKKSLAVAVY | NHYKRINSGS | KIDDVELSKS | NILMIGPTGS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GKTLLAQTLA | RILNVPFAIA | DATSLTEAGY | VGEDVENILL | KLIQAADYDV | ERAEKGIIYI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DEIDKIARKS | ENPSITRDVS | GEGVQQALLK | ILEGTIASVP | PQGGRKHPHQ | EFIQIDTTNI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LFICGGAFDG | LEPIIKRRLG | KKVIGFGADI | QQSDVDEKNL | LSKVLPEDLL | KFGLIPEFVG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RLPVITTLEP | LDEQALVDIL | TKPKNAIVKQ | YQKMLELDGV | ELEFEEEALR | EIAKKAIERK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TGARGLRSII | EGIMLDVMFE | LPSREDVQKC | IITVETVRGN | KPPKLIRHDG | TVIEQERKTS |
| A |