P50866
Gene name |
clpX |
Protein name |
ATP-dependent Clp protease ATP-binding subunit ClpX |
Names |
|
Species |
Bacillus subtilis (strain 168) |
KEGG Pathway |
bsu:BSU28220 |
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 P50866
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P50866-F1 | Predicted | AlphaFoldDB |
No variants for P50866
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P50866 | |||||
No associated diseases with P50866
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| HslUV protease complex | A protein complex that possesses ATP-dependent protease activity; consists of an ATPase large subunit with homology to other ClpX family ATPases and a peptidase small subunit related to the proteasomal beta-subunits of eukaryotes. In the E. coli complex, a double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. |
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). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cell division | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. |
| protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
| proteolysis involved in protein catabolic process | The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFKFNEEKGQ | LKCSFCGKTQ | DQVRKLVAGP | GVYICDECIE | LCTEIVEEEL | GTEEEVEFKD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VPKPQEIREI | LNEYVIGQDQ | AKKSLAVAVY | NHYKRINSNS | KVDDVELSKS | NISLIGPTGS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GKTLLAQTLA | RILNVPFAIA | DATSLTEAGY | VGEDVENILL | KLIQAADYDV | EKAEKGIIYI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DEIDKVARKS | ENPSITRDVS | GEGVQQALLK | ILEGTVASVP | PQGGRKHPHQ | EFIQIDTTNI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LFICGGAFDG | IEQIIKRRLG | QKVIGFGADN | KAADLEKEDL | LSKVLPEDLL | RFGLIPEFIG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RLPVIASLEK | LDEEALVAIL | TKPKNALVKQ | FKKMLELDNV | ELEFEEEALS | EIAKKAIERK |
| 370 | 380 | 390 | 400 | 410 | |
| TGARGLRSII | EGIMLDVMFE | LPSRDDIEKC | VITGATVTHG | EPPRLLLKDG | TEVSQDKTSA |