A8FFD2
Gene name |
dnaK |
Protein name |
Chaperone protein DnaK |
Names |
HSP70, Heat shock 70 kDa protein, Heat shock protein 70 |
Species |
Bacillus pumilus (strain SAFR-032) |
KEGG Pathway |
bpu:BPUM_2280 |
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 A8FFD2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A8FFD2-F1 | Predicted | AlphaFoldDB |
No variants for A8FFD2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A8FFD2 | |||||
No associated diseases with A8FFD2
3 regional properties for A8FFD2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Heat shock protein 70, conserved site | 7 - 14 | IPR018181-1 |
| conserved_site | Heat shock protein 70, conserved site | 166 - 179 | IPR018181-2 |
| conserved_site | Heat shock protein 70, conserved site | 307 - 321 | IPR018181-3 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 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. |
| unfolded protein binding | Binding to an unfolded protein. |
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 |
| MSKIIGIDLG | TTNSCVAVLE | GGEPKVIANA | EGARTTPSVV | AFKNGERQVG | EVAKRQSITN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PNTIMSVKRH | MGTDYKVEVE | GKNYTPQEIS | AIILQHLKSY | AEGYLGEEVT | KAVITVPAYF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NDAERQATKD | AGKIAGLEVE | RIINEPTAAA | LAYGLDKTDE | DQTILVYDLG | GGTFDVSVLE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LGDGVFEVRS | TAGDNRLGGD | DFDQVIIDHL | VAEFKKENGI | DLSKDKMALQ | RLKDAAEKAK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KDLSGVSSTQ | ISLPFITAGD | AGPLHLELTL | TRAKFEELSA | DLVERTMTPV | RQSLKDAGLS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ASEIDKVILV | GGSTRIPAVQ | EAIKKETGKE | PHKGVNPDEV | VALGAAIQGG | VITGDVKDVV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LLDVTPLSLG | IETMGGVFTK | LIERNTTIPT | SKSQVFSTAA | DNQTAVDIHV | LQGERPMAAD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NKTLGRFQLT | DIPPAPRGVP | QIEVSFDIDK | NGIVNVRAKD | MGTGKEQNIT | IKSSSGLSDD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EIEKMVKEAE | ENAEADAKKK | EEIEVRNEAD | QLVFTTEKTL | KDLEGKIDEE | QVKKANDAKD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ALKAAIEKGE | LEDIKAKKDE | LQTIVQELTT | KLYEEAAKQA | QAQQEGGAEG | AQKADDNVVD |
| 610 | |||||
| AEYEEVNDDQ | EKK |