Q8P855
Gene name |
htpG |
Protein name |
Chaperone protein HtpG |
Names |
Heat shock protein HtpG, High temperature protein G |
Species |
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) |
KEGG Pathway |
xcc:XCC2393 |
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 Q8P855
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8P855-F1 | Predicted | AlphaFoldDB |
No variants for Q8P855
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8P855 | |||||
No associated diseases with Q8P855
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
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. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to DNA damage stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. |
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| 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 |
| MTVDTDKQTL | GFQTEVKQLL | QLMIHSLYSN | KEIFLRELVS | NAADAADKLR | FEALVKPELL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EGSGELRIRV | DFDKEARTVT | IDDNGIGMSR | EDAVSHLGTI | AKSGTADFLK | HLSGDQKKDA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NLIGQFGVGF | YSAFIVADQV | DVYSRRAGLP | ASDGVHWSSR | GEGEFEVASV | DKPERGTRIV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LHLKDGEDSF | ADGWTLRNIL | KKYSDHIGLP | IEMRKEHYGE | DADKPAEPEW | EVVNRASALW |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TRPKSEIKDE | EYQEFYKHVA | HDAGNPLAWS | HNKVEGKLDY | TSLLFVPGRA | PFDLYHRDSA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KGLKLYVQRV | FIMDQAEQFL | PLYLRFIKGV | VDSADLSLNV | SREILQSGPV | VDSMKSALTK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RALDMLEKLA | KDKPDDYATF | WRNFGQALKE | GPAEDYANRE | KVAGLLRFSS | THDTTGAQSV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ALADYVGRMT | EGQDKLYYLT | GESYAQIKDS | PHLEVFRKKG | IEVLLLTDRI | DEWLMSYLTE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FDSKSFVDVA | RGDLDLGKLD | SEEDKKAQEE | VAKSKEGLAS | RIKAALGDDV | AEVRVSHRLT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DSPAILAIGQ | GDLGLQMRQL | LEASGQAVPE | TKPVFEFNPA | HPLIEKLDAE | QDMDRFGDLS |
| 610 | 620 | 630 | |||
| RVLFDQAALA | AGDSLKDPAG | YVRRLNKLLL | ELSA |