A4FPA5
Gene name |
groEL2 |
Protein name |
Chaperonin GroEL 2 |
Names |
60 kDa chaperonin 2, Chaperonin-60 2, Cpn60 2 |
Species |
Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338) |
KEGG Pathway |
sen:SACE_6714 |
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 A4FPA5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A4FPA5-F1 | Predicted | AlphaFoldDB |
No variants for A4FPA5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A4FPA5 | |||||
No associated diseases with A4FPA5
1 regional properties for A4FPA5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Chaperonin Cpn60, conserved site | 403 - 414 | 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 |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAKQIAFDEQ | ARRALERGVN | QLADAVKVTL | GPRGRHVVLD | KQFGGPQVTN | DGVTIAREIE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LEDPYENLGA | QLAKNVATKT | NDVAGDGTTT | ATVLAQAMVR | EGLRNLAAGA | NPTALGRGIQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AATDAVVDAL | KAKATPVKGR | DNIAQIATVS | SRDESIGALV | GEAMERVGED | GVISIEESST |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LATELEITEG | VQFDKGFVSP | YFVTDSERQE | AVLEDAQILL | HREKISSIQD | LLPLLEKIAQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SGKPLLILAE | DVEGEALSTL | VVNAIRKTFK | VVAVKAPYFG | DRRKAFLDDL | AAVTGAQVIA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PEVGLKLSEA | GPEVLGSARR | ITVTKDTTTI | VDGRGPQDDV | KARAEQIRKE | IEVSDSDWDR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EKLQERLAKL | AGGVAVIKVG | AATETELKER | KSRIEDAVAA | SKAAAEEGSV | PGGGSSLIHA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AKELNGDLGL | SGDEATGVRL | VRTALEAPLF | WIASNAGQEG | AVVVSKVRDL | DWGQGYNAAT |
| 490 | 500 | 510 | 520 | 530 | |
| LTFGDLVQPG | IVDPLKVTRS | AVANAASIAR | MVLTTESAVV | DKPEEEDSAA | AGHGHGHSH |