Q7WC32
Gene name |
htpG |
Protein name |
Chaperone protein HtpG |
Names |
Heat shock protein HtpG, High temperature protein G |
Species |
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253) |
KEGG Pathway |
bpa:BPP0496 |
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 Q7WC32
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7WC32-F1 | Predicted | AlphaFoldDB |
No variants for Q7WC32
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7WC32 | |||||
No associated diseases with Q7WC32
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 |
| MSQTTTNSAS | ETLGFQAEVK | QLLHLMIHSL | YSNKEIFLRE | LVSNASDACD | KLRFEAIDQP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GLLDGDGELA | IRVDYDKAAR | TITISDNGIG | LSRDEAVANL | GTIARSGTRE | FFSQLTGDKQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KDAQLIGQFG | VGFYSSFIVA | DKVTVLSRRA | GLAANEAIRW | ESDGQGEFSI | APAEKAGRGT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DVVLHLRADE | DELLNGWKLR | EILRRYSDHI | SLPIRMAKED | WDAEKGEQVK | GDELETVNQA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NALWTRNKSD | ITDEQYREFY | KTVSHDYDDP | LAWTHNRVEG | RSEYTQLLYV | PRHAPFDLWD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RDARRGVKLY | VKRVFIMDDA | EQLLPSYLRF | VRGVIDSADL | PLNVSREILQ | ESRDVRAIRE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GSAKRVLSLL | EDMAENKAED | YATFWTEFGQ | VLKEGTGEDA | ANRERIARLL | CFASTHDGEQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AQTVSFADYV | GRMKDGQDKI | YYVTADTFTA | AANSPHLEIF | RKKGIEVLLL | SDRVDEWMLS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YLREFDGKSL | VSVAKGGLDL | AELADEEEKK | RQSEVAETFK | PLVERLQQAL | AEQVKEVRVT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| QRLVDSPACV | VVGQNELSPH | LLRMLKAAGQ | EAPEVKPVLE | INPDHALIAR | IRDASDAEFG |
| 610 | 620 | 630 | |||
| DWAALLLDQA | LLAEGAQIAD | PAAFVKRLNG | LLLKA |