Q9I3C5
Gene name |
htpG |
Protein name |
Chaperone protein HtpG |
Names |
Heat shock protein HtpG, High temperature protein G |
Species |
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
KEGG Pathway |
pae:PA1596 |
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 Q9I3C5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9I3C5-F1 | Predicted | AlphaFoldDB |
No variants for Q9I3C5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9I3C5 | |||||
No associated diseases with Q9I3C5
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 |
| MSVETQKETL | GFQTEVKQLL | HLMIHSLYSN | KEIFLRELIS | NASDAADKLR | FEALANPELL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EGGAELKIRV | SFDKEANTVT | LEDNGIGMSR | EDVVTHLGTI | AKSGTADFLK | NLSGDQKKDS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HLIGQFGVGF | YSAFIVADKV | DVYSRRAGQP | ASEGVHWSSK | GEGEFDVATI | DKPERGTRIV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LHLKKGEEEF | ADGWRLRNVI | KKYSDHIALP | IELPKEFHGE | EADKPAEPEW | ETVNRASALW |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TRPRAEVKDE | EYQEFYKHVA | HDFENPLSWS | HNKVEGKLEY | TSLLYVPGRA | PFDLYHREAP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RGLKLYVQRV | FIMDQADEFL | PLYLRFIKGV | VDSNDLSLNV | SREILQKDPV | IDSMKSALTK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RVLDMLEKLA | KNEPEQYKTF | WKNFGQVLKE | GPAEDFGNKE | KIAGLLRFAS | TGDDSGEQSV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ALADYIGRMK | EGQDKIYYLT | GESYSQVKNS | PHLEVFRKKG | IEVLLLTDRI | DEWLMSYLPE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FDGKQFVDVA | RGDLDLGSLD | SEEDKKAQEE | VAKSKEGLIE | RLKKVLDEQV | SEVRVSHRLT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DSPAILAIGE | QDLGLQMRQI | LEASGQKVPD | SKPIFEINPQ | HPLIEKLDAE | PDEDRFGELS |
| 610 | 620 | 630 | |||
| HILFDQAALA | AGDSLKDPGA | YVRRLNKLLV | ELSA |