Q2FDW8
Gene name |
glcB (SAUSA300_2476) |
Protein name |
PTS system glucoside-specific EIICBA component |
Names |
|
Species |
Staphylococcus aureus (strain USA300) |
KEGG Pathway |
saa:SAUSA300_2476 |
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 Q2FDW8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2FDW8-F1 | Predicted | AlphaFoldDB |
No variants for Q2FDW8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2FDW8 | |||||
No associated diseases with Q2FDW8
6 regional properties for Q2FDW8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phosphotransferase system, sugar-specific permease EIIA type 1 | 543 - 666 | IPR001127 |
| domain | Phosphotransferase system, IIB component, type 1 | 416 - 519 | IPR001996 |
| domain | Phosphotransferase system, EIIC | 13 - 356 | IPR003352 |
| domain | PTS system glucose-specific IIBC component | 2 - 515 | IPR011299 |
| domain | Phosphotransferase system, EIIC component, type 1 | 3 - 427 | IPR013013 |
| conserved_site | Phosphotransferase system EIIB, cysteine phosphorylation site | 443 - 513 | IPR018113 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| 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 |
|---|---|
| glucose transmembrane transporter activity | Enables the transfer of the hexose monosaccharide glucose from one side of a membrane to the other. |
| kinase activity | Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. |
| protein-N(PI)-phosphohistidine-sugar phosphotransferase activity | Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + sugar(out) = protein histidine + sugar phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| phosphoenolpyruvate-dependent sugar phosphotransferase system | The uptake and phosphorylation of specific carbohydrates from the extracellular environment; uptake and phosphorylation are coupled, making the PTS a link between the uptake and metabolism of sugars; phosphoenolpyruvate is the original phosphate donor; phosphoenolpyruvate passes the phosphate via a signal transduction pathway, to enzyme 1 (E1), which in turn passes it on to the histidine protein, HPr; the next step in the system involves sugar-specific membrane-bound complex, enzyme 2 (EII), which transports the sugar into the cell; it includes the sugar permease, which catalyzes the transport reactions; EII is usually divided into three different domains, EIIA, EIIB, and EIIC. |
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFKKLFGQLQ | RIGKALMLPV | AILPAAGILL | AFGNAMHNEQ | LVEIAPWLKN | DIIVMISSVM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EAAGQVVFDN | LPLLFAVGTA | LGLAGGDGVA | ALAALVGYLI | MNATMGKVLH | ITIDDIFSYA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KGAKELSQAA | KEPAHALVLG | IPTLQTGVFG | GIIMGALAAW | CYNKFYNITL | PPFLGFFAGK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RFVPIVTSVV | AIATGVLLSF | AWPPIQDGLN | SLSNFLLNKN | LTLTTFIFGI | IERSLIPFGL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HHIFYSPFWF | EFGSYTNHAG | ELVRGDQRIW | MAQLKDGVPF | TAGAFTTGKY | PFMMFGLPAA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AFAIYKNARP | ERKKVVGGLM | LSAGLTAFLT | GITEPLEFSF | LFVAPVLYGI | HVLLAGTSFL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VMHLLGVKIG | MTFSGGFIDY | ILYGLLNWDR | SHALLVIPVG | IVYAIVYYFL | FDFAIRKFKL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KTPGREDEET | EIRNSSVAKL | PFDVLDAMGG | KENIKHLDAC | ITRLRVEVVD | KSKVDVAGIK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ALGASGVLEV | GNNMQAIFGP | KSDQIKHDMA | KIMSGEITKP | SETTVTEEMS | DEPVHVEALG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| TTDIYAPGIG | QIIPLSEVPD | QVFAGKMMGD | GVGFIPEKGE | IVAPFDGTVK | TIFPTKHAIG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LESESGVEVL | IHIGIDTVKL | NGEGFESLIN | VDEKVTQGQP | LMKVNLAYLK | AHAPSIVTPM |
| 670 | 680 | ||||
| IITNLENKEL | VIEDVQDADP | GKLIMTVK |