P69798
Gene name |
manX (c2223) |
Protein name |
PTS system mannose-specific EIIAB component |
Names |
EIIAB-Man, EIII-Man |
Species |
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) |
KEGG Pathway |
ecc:c2223 |
EC number |
2.7.1.191: Phosphotransferases with an alcohol group as acceptor |
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 P69798
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P69798-F1 | Predicted | AlphaFoldDB |
No variants for P69798
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P69798 | |||||
No associated diseases with P69798
4 regional properties for P69798
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phosphotransferase system, mannose-type IIA component | 2 - 126 | IPR004701 |
| domain | Phosphotransferase system, sorbose subfamily IIB component | 160 - 323 | IPR004720 |
| domain | Phosphotransferase system, mannose family IIA component | 2 - 117 | IPR013789 |
| domain | PTS system mannose/sorbose specific IIA subunit | 3 - 124 | IPR033887 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.1.191 | Phosphotransferases with an alcohol group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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 |
| MTIAIVIGTH | GWAAEQLLKT | AEMLLGEQEN | VGWIDFVPGE | NAETLIEKYN | AQLAKLDTTK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GVLFLVDTWG | GSPFNAASRI | VVDKEHYEVI | AGVNIPMLVE | TLMARDDDPS | FDELVALAVE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TGREGVKALK | AKPVEKAAPA | PAAAAPKAAP | TPAKPMGPND | YMVIGLARID | DRLIHGQVAT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RWTKETNVSR | IIVVSDEVAA | DTVRKTLLTQ | VAPPGVTAHV | VDVAKMIRVY | NNPKYAGERV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MLLFTNPTDV | ERLVEGGVKI | TSVNVGGMAF | RQGKTQVNNA | VSVDEKDIEA | FKKLNARGIE |
| 310 | 320 | ||||
| LEVRKVSTDP | KLKMMDLISK | IDK |