P9WHV9
Gene name |
ppk |
Protein name |
Polyphosphate kinase |
Names |
ATP-polyphosphate phosphotransferase, Polyphosphoric acid kinase |
Species |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
KEGG Pathway |
mtu:Rv2984 |
EC number |
2.7.4.1: Phosphotransferases with a phosphate 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 P9WHV9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P9WHV9-F1 | Predicted | AlphaFoldDB |
No variants for P9WHV9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P9WHV9 | |||||
No associated diseases with P9WHV9
4 regional properties for P9WHV9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Polyphosphate kinase middle domain | 168 - 376 | IPR024953 |
| domain | Polyphosphate kinase N-terminal domain | 53 - 159 | IPR025198 |
| domain | Polyphosphate kinase C-terminal domain 2 | 559 - 726 | IPR025200 |
| domain | Polyphosphate kinase, C-terminal domain 1 | 386 - 552 | IPR041108 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.4.1 | Phosphotransferases with a phosphate group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| polyphosphate kinase complex | A protein complex that possesses polyphosphate kinase activity. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| polyphosphate kinase activity | Catalysis of the reaction: ATP + phosphate(n) = ADP + phosphate(n+1). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| polyphosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of a polyphosphate, the anion or salt of polyphosphoric acid. |
| protein autophosphorylation | The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). |
| stringent response | A specific global change in the metabolism of a bacterial cell (the downregulation of nucleic acid and protein synthesis, and the simultaneous upregulation of protein degradation and amino acid synthesis) as a result of starvation. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MMSNDRKVTE | IENSPVTEVR | PEEHAWYPDD | SALAAPPAAT | PAAISDQLPS | DRYLNRELSW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LDFNARVLAL | AADKSMPLLE | RAKFLAIFAS | NLDEFYMVRV | AGLKRRDEMG | LSVRSADGLT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PREQLGRIGE | QTQQLASRHA | RVFLDSVLPA | LGEEGIYIVT | WADLDQAERD | RLSTYFNEQV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FPVLTPLAVD | PAHPFPFVSG | LSLNLAVTVR | QPEDGTQHFA | RVKVPDNVDR | FVELAAREAS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EEAAGTEGRT | ALRFLPMEEL | IAAFLPVLFP | GMEIVEHHAF | RITRNADFEV | EEDRDEDLLQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ALERELARRR | FGSPVRLEIA | DDMTESMLEL | LLRELDVHPG | DVIEVPGLLD | LSSLWQIYAV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DRPTLKDRTF | VPATHPAFAE | RETPKSIFAT | LREGDVLVHH | PYDSFSTSVQ | RFIEQAAADP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NVLAIKQTLY | RTSGDSPIVR | ALIDAAEAGK | QVVALVEIKA | RFDEQANIAW | ARALEQAGVH |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VAYGLVGLKT | HCKTALVVRR | EGPTIRRYCH | VGTGNYNSKT | ARLYEDVGLL | TAAPDIGADL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| TDLFNSLTGY | SRKLSYRNLL | VAPHGIRAGI | IDRVEREVAA | HRAEGAHNGK | GRIRLKMNAL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VDEQVIDALY | RASRAGVRIE | VVVRGICALR | PGAQGISENI | IVRSILGRFL | EHSRILHFRA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| IDEFWIGSAD | MMHRNLDRRV | EVMAQVKNPR | LTAQLDELFE | SALDPCTRCW | ELGPDGQWTA |
| 730 | 740 | ||||
| SPQEGHSVRD | HQESLMERHR | SP |