Q9WY63
Gene name |
fliG (TM_0220) |
Protein name |
Flagellar motor switch protein FliG |
Names |
|
Species |
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
KEGG Pathway |
tma:TM0220 |
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
8 structures for Q9WY63
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1LKV | X-ray | 280 A | X | 104-335 | PDB |
| 1QC7 | X-ray | 220 A | A/B | 235-335 | PDB |
| 3AJC | X-ray | 230 A | A | 104-335 | PDB |
| 3SOH | X-ray | 350 A | B/D | 117-193 | PDB |
| 4FHR | X-ray | 193 A | B | 115-327 | PDB |
| 4QRM | X-ray | 432 A | B/D/F/H/J/L/N/P/R/T/V | 117-187 | PDB |
| 5TDY | X-ray | 210 A | B/D | 1-98 | PDB |
| AF-Q9WY63-F1 | Predicted | AlphaFoldDB |
No variants for Q9WY63
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9WY63 | |||||
No associated diseases with Q9WY63
3 regional properties for Q9WY63
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| bacterial-type flagellum basal body | One of the three major substructures of the bacterial-type flagellum, the basal body is embedded in the cell envelope (the plasma membrane, peptidoglycan cell wall, and, if one is present, the outer membrane); it houses the secretion apparatus that exports the more distal components and the flagellar motor. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| cytoskeletal motor activity | Generation of force resulting in movement, for example along a microfilament or microtubule, or in torque resulting in membrane scission or rotation of a flagellum. The energy required is obtained either from the hydrolysis of a nucleoside triphosphate or by an electrochemical proton gradient (proton-motive force). |
| protein heterodimerization activity | Binding to a nonidentical protein to form a heterodimer. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| bacterial-type flagellum-dependent cell motility | Cell motility due to the motion of one or more bacterial-type flagella. A bacterial-type flagellum is a motor complex composed of an extracellular helical protein filament coupled to a rotary motor embedded in the cell envelope. |
| chemotaxis | The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPEKKIDGRR | KAAVLLVALG | PEKAAQVMKH | LDEETVEQLV | VEIANIGRVT | PEEKKQVLEE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FLSLAKAKEM | ISEGGIEYAK | KVLEKAFGPE | RARKIIERLT | SSLQVKPFSF | VRDTDPVQLV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NFLQSEHPQT | IAVVLSYLDP | PVAAQILGAL | PEELQTEVLK | RIALLERTSP | EVVKEIERNL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EKKISGFVSR | TFSKVGGIDT | AAEIMNNLDR | TTEKKIMDKL | VQENPELADE | IRRRMFVFED |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ILKLDDRSIQ | LVLREVDTRD | LALALKGASD | ELKEKIFKNM | SKRAAALLKD | ELEYMGPVRL |
| 310 | 320 | 330 | |||
| KDVEEAQQKI | INIIRRLEEA | GEIVIARGGG | EELIM |