P42383
Gene name |
groEL |
Protein name |
Chaperonin GroEL |
Names |
60 kDa chaperonin, Chaperonin-60, Cpn60 |
Species |
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
KEGG Pathway |
hpy:HP_0010 |
EC number |
5.6.1.7: Enzymes altering polypeptide conformation or assembly |
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 P42383
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P42383-F1 | Predicted | AlphaFoldDB |
4 variants for P42383
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| 76 | V>D | strain: 85P [UniProt] | No | ||
| 123 | A>P | strain: 85P [UniProt] | No | ||
| 293 | I>V | strain: 85P [UniProt] | No | ||
| 320 | G>K | strain: 85P [UniProt] | No |
No associated diseases with P42383
1 regional properties for P42383
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Chaperonin Cpn60, conserved site | 404 - 415 | IPR018370 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.6.1.7 | Enzymes altering polypeptide conformation or assembly |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| GroEL-GroES complex | Bacterial chaperonin complex consisting of a heptameric 10kDa chaperonin subunit GroES and a tetradecameric (2x7) 60kDa chaperonin subunit GroEL. The 60kDa subunit possesses ATPase activity while the holo-enzyme is responsible for the correct folding of proteins. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| isomerase activity | Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5. |
| unfolded protein binding | Binding to an unfolded protein. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| chaperone cofactor-dependent protein refolding | The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release. |
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| protein refolding | The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. |
| response to heat | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAKEIKFSDS | ARNLLFEGVR | QLHDAVKVTM | GPRGRNVLIQ | KSYGAPSITK | DGVSVAKEIE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LSCPVANMGA | QLVKEVASKT | ADAAGDGTTT | ATVLAYSIFK | EGLRNITAGA | NPIEVKRGMD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KAAEAIINEL | KKASKKVGGK | EEITQVATIS | ANSDHNIGKL | IADAMEKVGK | DGVITVEEAK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GIEDELDVVE | GMQFDRGYLS | PYFVTNAEKM | TAQLDNAYIL | LTDKKISSMK | DILPLLEKTM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KEGKPLLIIA | EDIEGEALTT | LVVNKLRGVL | NIAAVKAPGF | GDRRKEMLKD | IAILTGGQVI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SEELGLSLEN | AEVEFLGKAG | RIVIDKDNTT | IVDGKGHSHD | VKDRVAQIKT | QIASTTSDYD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KEKLQERLAK | LSGGVAVIKV | GAASEVEMKE | KKDRVDDALS | ATKAAVEEGI | VIGGGAALIR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AAQKVHLNLH | DDEKVGYEII | MRAIKAPLAQ | IAINAGYDGG | VVVNEVEKHE | GHFGFNASNG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KYVDMFKEGI | IDPLKVERIA | LQNAVSVSSL | LLTTEATVHE | IKEEKAAPAM | PDMGGMGGMG |
| GMGGMM |