P0AG24
Gene name |
spoT (b3650, JW3625) |
Protein name |
Bifunctional (p)ppGpp synthase/hydrolase SpoT |
Names |
|
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b3650 |
EC number |
2.7.6.5: Diphosphotransferases |
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 P0AG24
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0AG24-F1 | Predicted | AlphaFoldDB |
No variants for P0AG24
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0AG24 | |||||
No associated diseases with P0AG24
7 regional properties for P0AG24
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ACT domain | 622 - 702 | IPR002912 |
| domain | HD/PDEase domain | 41 - 166 | IPR003607 |
| domain | TGS | 386 - 447 | IPR004095 |
| domain | HD domain | 45 - 144 | IPR006674 |
| domain | RelA/SpoT | 214 - 345 | IPR007685 |
| domain | RelA/SpoT, TGS domain | 389 - 447 | IPR033655 |
| domain | RelA/SpoT, AH and RIS domains | 459 - 541 | IPR045600 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.6.5 | Diphosphotransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTP diphosphokinase activity | Catalysis of the reaction: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate. |
| guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity | Catalysis of the reaction: guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate. |
| kinase activity | Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| guanosine tetraphosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of guanine tetraphosphate (5'-ppGpp-3'), a derivative of guanine riboside with four phosphates. |
| guanosine tetraphosphate metabolic process | The chemical reactions and pathways involving guanine tetraphosphate (5'-ppGpp-3'), a derivative of guanine riboside with four phosphates. |
| nucleobase-containing small molecule interconversion | The chemical reactions and pathways by which a nucleobase, nucleoside or nucleotide small molecule is synthesized from another nucleobase, nucleoside or nucleotide small molecule. |
| phosphorylation | The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide. |
| response to starvation | 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 starvation stimulus, deprivation of nourishment. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MYLFESLNQL | IQTYLPEDQI | KRLRQAYLVA | RDAHEGQTRS | SGEPYITHPV | AVACILAEMK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LDYETLMAAL | LHDVIEDTPA | TYQDMEQLFG | KSVAELVEGV | SKLDKLKFRD | KKEAQAENFR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KMIMAMVQDI | RVILIKLADR | THNMRTLGSL | RPDKRRRIAR | ETLEIYSPLA | HRLGIHHIKT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ELEELGFEAL | YPNRYRVIKE | VVKAARGNRK | EMIQKILSEI | EGRLQEAGIP | CRVSGREKHL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YSIYCKMVLK | EQRFHSIMDI | YAFRVIVNDS | DTCYRVLGQM | HSLYKPRPGR | VKDYIAIPKA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NGYQSLHTSM | IGPHGVPVEV | QIRTEDMDQM | AEMGVAAHWA | YKEHGETSTT | AQIRAQRWMQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SLLELQQSAG | SSFEFIESVK | SDLFPDEIYV | FTPEGRIVEL | PAGATPVDFA | YAVHTDIGHA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| CVGARVDRQP | YPLSQPLTSG | QTVEIITAPG | ARPNAAWLNF | VVSSKARAKI | RQLLKNLKRD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DSVSLGRRLL | NHALGGSRKL | NEIPQENIQR | ELDRMKLATL | DDLLAEIGLG | NAMSVVVAKN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LQHGDASIPP | ATQSHGHLPI | KGADGVLITF | AKCCRPIPGD | PIIAHVSPGK | GLVIHHESCR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NIRGYQKEPE | KFMAVEWDKE | TAQEFITEIK | VEMFNHQGAL | ANLTAAINTT | TSNIQSLNTE |
| 670 | 680 | 690 | 700 | ||
| EKDGRVYSAF | IRLTARDRVH | LANIMRKIRV | MPDVIKVTRN | RN |