P9WI81
Gene name |
pknB (Rv0014c, MTCY10H4.14c) |
Protein name |
Serine/threonine-protein kinase PknB |
Names |
|
Species |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
KEGG Pathway |
mtu:Rv0014c |
EC number |
2.7.11.1: Protein-serine/threonine kinases |
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
25 structures for P9WI81
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1MRU | X-ray | 300 A | A/B | 1-308 | PDB |
| 1O6Y | X-ray | 220 A | A | 1-279 | PDB |
| 2FUM | X-ray | 289 A | A/B/C/D | 1-279 | PDB |
| 2KUD | NMR | - | A | 355-491 | PDB |
| 2KUE | NMR | - | A | 423-557 | PDB |
| 2KUF | NMR | - | A | 491-626 | PDB |
| 2KUI | NMR | - | A | 355-626 | PDB |
| 3F61 | X-ray | 180 A | A | 1-308 | PDB |
| 3F69 | X-ray | 280 A | A/B | 1-308 | PDB |
| 3ORI | X-ray | 200 A | A/B/C/D | 1-308 | PDB |
| 3ORK | X-ray | 160 A | A | 1-308 | PDB |
| 3ORL | X-ray | 290 A | A | 1-308 | PDB |
| 3ORM | X-ray | 250 A | A | 1-308 | PDB |
| 3ORO | X-ray | 190 A | A | 1-308 | PDB |
| 3ORP | X-ray | 210 A | A | 1-308 | PDB |
| 3ORT | X-ray | 190 A | A | 1-308 | PDB |
| 3OUV | X-ray | 200 A | A | 489-558 | PDB |
| 5E0Y | X-ray | 200 A | A | 558-626 | PDB |
| 5E0Z | X-ray | 200 A | A | 491-626 | PDB |
| 5E10 | X-ray | 180 A | A | 360-491 | PDB |
| 5E12 | X-ray | 221 A | A/B | 423-626 | PDB |
| 5U94 | X-ray | 220 A | A | 1-280 | PDB |
| 6B2P | X-ray | 301 A | A | 1-279 | PDB |
| 6I2P | X-ray | 237 A | A/B | 1-279 | PDB |
| AF-P9WI81-F1 | Predicted | AlphaFoldDB |
No variants for P9WI81
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P9WI81 | |||||
No associated diseases with P9WI81
7 regional properties for P9WI81
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 11 - 274 | IPR000719 |
| domain | PASTA domain | 356 - 422 | IPR005543-1 |
| domain | PASTA domain | 423 - 490 | IPR005543-2 |
| domain | PASTA domain | 491 - 557 | IPR005543-3 |
| domain | PASTA domain | 558 - 626 | IPR005543-4 |
| active_site | Serine/threonine-protein kinase, active site | 134 - 146 | IPR008271 |
| binding_site | Protein kinase, ATP binding site | 17 - 40 | IPR017441 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.11.1 | Protein-serine/threonine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| 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. |
| peptidoglycan-based cell wall | A protective structure outside the cytoplasmic membrane composed of peptidoglycan (also known as murein), a molecule made up of a glycan (sugar) backbone of repetitively alternating N-acetylglucosamine and N-acetylmuramic acid with short, attached, cross-linked peptide chains containing unusual amino acids. An example of this component is found in Escherichia coli. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetyltransferase activator activity | Binds to and increases the activity of an acetyltransferase, an enzyme which catalyzes the transfer of an acetyl group to an acceptor molecule. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| identical protein binding | Binding to an identical protein or proteins. |
| manganese ion binding | Binding to a manganese ion (Mn). |
| protein kinase activity | Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. |
| protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
| protein serine/threonine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. |
12 GO annotations of biological process
| Name | Definition |
|---|---|
| negative regulation of catalytic activity | Any process that stops or reduces the activity of an enzyme. |
| negative regulation of fatty acid biosynthetic process | Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of fatty acids. |
| negative regulation of growth rate | Any process that reduces the rate of growth of all or part of an organism. |
| negative regulation of protein binding | Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding. |
| peptidoglycan biosynthetic process | The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls. |
| peptidyl-serine phosphorylation | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. |
| positive regulation of catalytic activity | Any process that activates or increases the activity of an enzyme. |
| positive regulation of DNA binding | Any process that increases the frequency, rate or extent of DNA binding. DNA binding is any process in which a gene product interacts selectively with DNA (deoxyribonucleic 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). |
| protein phosphorylation | The process of introducing a phosphate group on to a protein. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
| response to host immune response | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detecting the immune response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTTPSHLSDR | YELGEILGFG | GMSEVHLARD | LRLHRDVAVK | VLRADLARDP | SFYLRFRREA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QNAAALNHPA | IVAVYDTGEA | ETPAGPLPYI | VMEYVDGVTL | RDIVHTEGPM | TPKRAIEVIA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DACQALNFSH | QNGIIHRDVK | PANIMISATN | AVKVMDFGIA | RAIADSGNSV | TQTAAVIGTA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QYLSPEQARG | DSVDARSDVY | SLGCVLYEVL | TGEPPFTGDS | PVSVAYQHVR | EDPIPPSARH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EGLSADLDAV | VLKALAKNPE | NRYQTAAEMR | ADLVRVHNGE | PPEAPKVLTD | AERTSLLSSA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AGNLSGPRTD | PLPRQDLDDT | DRDRSIGSVG | RWVAVVAVLA | VLTVVVTIAI | NTFGGITRDV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QVPDVRGQSS | ADAIATLQNR | GFKIRTLQKP | DSTIPPDHVI | GTDPAANTSV | SAGDEITVNV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| STGPEQREIP | DVSTLTYAEA | VKKLTAAGFG | RFKQANSPST | PELVGKVIGT | NPPANQTSAI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TNVVIIIVGS | GPATKDIPDV | AGQTVDVAQK | NLNVYGFTKF | SQASVDSPRP | AGEVTGTNPP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AGTTVPVDSV | IELQVSKGNQ | FVMPDLSGMF | WVDAEPRLRA | LGWTGMLDKG | ADVDAGGSQH |
| 610 | 620 | ||||
| NRVVYQNPPA | GTGVNRDGII | TLRFGQ |