P45617
Gene name |
ptsI (MCAP_0233) |
Protein name |
Phosphoenolpyruvate-protein phosphotransferase |
Names |
Phosphotransferase system, enzyme I |
Species |
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154) |
KEGG Pathway |
mcp:MCAP_0233 |
EC number |
2.7.3.9: Phosphotransferases with a nitrogenous 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 P45617
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P45617-F1 | Predicted | AlphaFoldDB |
No variants for P45617
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P45617 | |||||
No associated diseases with P45617
6 regional properties for P45617
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PEP-utilising enzyme, C-terminal | 252 - 541 | IPR000121 |
| domain | Phosphotransferase system, enzyme I-like | 5 - 566 | IPR006318 |
| domain | PEP-utilising enzyme, mobile domain | 153 - 226 | IPR008279 |
| domain | Phosphotransferase system, enzyme I N-terminal | 6 - 127 | IPR008731 |
| active_site | PEP-utilising enzyme, active site | 185 - 196 | IPR018274 |
| conserved_site | PEP-utilising enzyme, conserved site | 447 - 465 | IPR023151 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.3.9 | Phosphotransferases with a nitrogenous group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| kinase activity | Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. |
| metal ion binding | Binding to a metal ion. |
| phosphoenolpyruvate-protein phosphotransferase activity | Catalysis of the reaction: phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine. |
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 |
| MSKQIKGIAA | SEGISLARAL | VIKETKLDIQ | KQLISDVDQE | IIKLEQAIEK | SIADLKKIQQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ITLKKLGEEK | AAIFDAHQDI | ANDPAIKEEV | VELIKKEKVN | AEYALFTVSN | NYFEMFSQLE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DPYFKERSAD | IKDVSLRIIS | HILGLEIHDL | STIDKEVIII | SDDLTPSQTA | QLDKKFVKGF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LTNVGGRTSH | AAIMARSLEI | PAILGLKNIT | ELVKTDDLIA | LDGSSGIVEL | DLNDDDIKNY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QTKVQQYIEL | KEQLKKFKDE | PSLTKDKIKK | LIEANIGSTN | DVQSVLDSGA | EGIGLFRTEF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LYMDNDHFPT | EEEQFEAYKK | VVSQIKHLVV | FRTLDIGGDK | KLSYFKFDEE | MNPFLGYRAI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RFTLDRKDIF | KDQIRALLRA | SAFGKLGIMF | PMIATIDEFK | QAKTFVEECK | IELDKEGIKY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DNQVQIGMMV | EIPSAAILAD | QFAKYADFFS | IGTNDLIQYS | FASDRMNQNV | SYLYQPLNPS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LLRLIQLTIS | GAHKHNKWVG | MCGEMAGDSK | ALPILLGLDL | DAFSMSATSV | LKARSLMSKI |
| 550 | 560 | 570 | |||
| EFSKAKILAN | KVLECETNEQ | VNKLVEDFLN | NLD |