Q0S467
Gene name |
htpG |
Protein name |
Chaperone protein HtpG |
Names |
Heat shock protein HtpG, High temperature protein G |
Species |
Rhodococcus jostii (strain RHA1) |
KEGG Pathway |
rha:RHA1_ro05892 |
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 Q0S467
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q0S467-F1 | Predicted | AlphaFoldDB |
No variants for Q0S467
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q0S467 | |||||
No associated diseases with Q0S467
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 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. |
| 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 |
| MSTKIEQLEF | QAETRQLLDL | MIHSVYSNKD | SFLRELISNA | SDALDKLRLE | AFRNKELHVD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TSDLHVEIEV | DAEKRTLTVR | DNGIGMSHDE | VVDLIGTLAK | SGTADLRRKL | KEAKDAAASE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ELIGQFGIGF | YSTFMVADKV | TLLTRKAGES | EATRWESSGE | ATYTIEAVDD | APQGSSVTLH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LKPEDAEDHL | HDYTSERKIK | ELVKRYSDFI | AWPIRMNVER | TVPAEGDGED | EVTTTSETIN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SMKALWARSK | DDVSEDEYKE | FYKHIAHAWD | DPLEVIPMKA | EGTFEFQALL | FIPSHAPFDL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FMRDGKTGVQ | LYVKRVFIMD | DCDQLMPEYL | RFVKGVVDAQ | DLSLNVSREI | LQQDRQIRAI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RRRLTKKVLT | TIKDLKTERP | DDYRTFWAEF | GRAVKEGLMS | DTDNRDVLLG | ISSFASTHSE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EELTSLEDYV | ARMKDGQEQI | FYATGESRQL | LESSPHMEAF | RAKGFEVLLL | TDPVDEMWVG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AVPEFDGKSF | QSIAKGEVDL | DTEEDKKAHE | SEREEQEKDF | AGLLSWMADA | LSEQVKEVRL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| STRLTTSPAC | IVGDAFSMSP | ALERMYRASG | QPVPVTKRIL | ELNPTHPLVT | GLREAHGERN |
| 610 | 620 | 630 | 640 | ||
| EDPALGETAE | LLYGMALLAE | GGELEDPARF | TTMLANRLAR | TV |