UniProtKB - P9WI83 (PKNA_MYCTU)
Serine/threonine-protein kinase PknA
pknA
Functioni
Protein kinase that regulates many aspects of mycobacterial physiology, and is critical for growth in vitro and survival of the pathogen in the host (PubMed:25713147).
Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins such as FtsZ, Wag31, GlmU, FhaB, PstP, EmbR and Rv1422 (PubMed:15985609, PubMed:16817899, PubMed:19121323, PubMed:20066037, PubMed:21190553, PubMed:21423706).
Also catalyzes the phosphorylation of the proteasome alpha-subunit (PrcA) and unprocessed proteasome beta-subunit (pre-PrcB), which results in the inhibition of processing of pre-PrcB and assembly of the proteasome complex, and thereby enhances the mycobacterial resistance to H2O2; PknA thus plays an important role in the oxidative stress response by impeding the formation of holo-proteasome in M.tuberculosis under H2O2 stress (PubMed:25224505).
Shows a strong preference for Thr versus Ser as the phosphoacceptor.
8 PublicationsMiscellaneous
Catalytic activityi
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 42 | ATPPROSITE-ProRule annotation | 1 | |
Active sitei | 141 | Proton acceptorPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 19 – 27 | ATPPROSITE-ProRule annotation | 9 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- protein kinase activity Source: MTBBASE
- protein serine/threonine/tyrosine kinase activity Source: RHEA
- protein serine/threonine kinase activity Source: MTBBASE
- protein serine kinase activity Source: RHEA
GO - Biological processi
- negative regulation of catalytic activity Source: MTBBASE
- negative regulation of fatty acid biosynthetic process Source: MTBBASE
- negative regulation of lipid biosynthetic process Source: MTBBASE
- peptidyl-threonine autophosphorylation Source: CACAO
- positive regulation of catalytic activity Source: MTBBASE
- positive regulation of DNA binding Source: MTBBASE
- protein autophosphorylation Source: MTBBASE
- protein phosphorylation Source: MTBBASE
- regulation of cell shape Source: MTBBASE
Keywordsi
Molecular function | Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | Virulence |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 3445 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:pknA Ordered Locus Names:Rv0015c ORF Names:MTCY10H4.15c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv0015c |
Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication; Single-pass membrane protein 1 Publication
Note: The majority of the cells displays PknA expression at the membrane perimeter along the length of the cell, whereas a minor population shows PknA to localize at either or both poles (uni- and bipolar; 16 and 14%, respectively) and occasionally to both the poles and the midcell (12%).1 Publication
Cytosol
- cytosol Source: MTBBASE
Extracellular region or secreted
- extracellular region Source: MTBBASE
Plasma Membrane
- plasma membrane Source: MTBBASE
Other locations
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 339 | CytoplasmicSequence analysisAdd BLAST | 339 | |
Transmembranei | 340 – 360 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 361 – 431 | ExtracellularSequence analysisAdd BLAST | 71 |
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 42 | K → M: Loss of autophosphorylation activity. This mutation results in cell death. 2 Publications | 1 | |
Mutagenesisi | 172 | T → A: 10-fold reduction in transphosphorylation activity. This mutant strain shows severely compromised growth. Loss of autophosphorylation activity and weak transphosphorylation activity; when associated with A-174. 2 Publications | 1 | |
Mutagenesisi | 174 | T → A: 5-fold reduction in transphosphorylation activity. Loss of autophosphorylation activity and weak transphosphorylation activity; when associated with A-172. 2 Publications | 1 | |
Mutagenesisi | 180 | T → A: Loss of auto- and transphosphorylation activity. 2 Publications | 1 | |
Mutagenesisi | 180 | T → E: Loss of transphosphorylation activity. 1 Publication | 1 | |
Mutagenesisi | 180 | T → S: 4-fold reduction in transphosphorylation activity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL4295585 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000171205 | 1 – 431 | Serine/threonine-protein kinase PknAAdd BLAST | 431 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 8 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 10 | Phosphoserine; by autocatalysis1 Publication | 1 | |
Modified residuei | 21 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 46 | Phosphoserine; by autocatalysis1 Publication | 1 | |
Modified residuei | 64 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 65 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 75 | Phosphoserine; by autocatalysis1 Publication | 1 | |
Modified residuei | 90 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 105 | Phosphoserine; by autocatalysis1 Publication | 1 | |
Modified residuei | 125 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 152 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 158 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 172 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 174 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 180 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 198 | Phosphoserine; by autocatalysis1 Publication | 1 | |
Modified residuei | 224 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 252 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 263 | Phosphoserine; by autocatalysis1 Publication | 1 | |
Modified residuei | 302 | Phosphothreonine; by autocatalysis1 Publication | 1 | |
Modified residuei | 309 | Phosphoserine; by autocatalysis1 Publication | 1 | |
Modified residuei | 313 | Phosphothreonine; by autocatalysis1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDbi | P9WI83 |
PTM databases
iPTMneti | P9WI83 |
Expressioni
Inductioni
Interactioni
Protein-protein interaction databases
IntActi | P9WI83, 2 interactors |
STRINGi | 83332.Rv0015c |
Chemistry databases
BindingDBi | P9WI83 |
Structurei
Secondary structure
3D structure databases
SMRi | P9WI83 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 13 – 272 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 260 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 162 – 184 | Activation loop1 PublicationAdd BLAST | 23 | |
Regioni | 276 – 333 | DisorderedSequence analysisAdd BLAST | 58 | |
Regioni | 366 – 418 | DisorderedSequence analysisAdd BLAST | 53 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 302 – 316 | Polar residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 366 – 394 | Polar residuesSequence analysisAdd BLAST | 29 | |
Compositional biasi | 403 – 417 | Polar residuesSequence analysisAdd BLAST | 15 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | COG0515, Bacteria |
OMAi | CPGAPTT |
PhylomeDBi | P9WI83 |
Family and domain databases
InterProi | View protein in InterPro IPR011009, Kinase-like_dom_sf IPR000719, Prot_kinase_dom IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF00069, Pkinase, 1 hit |
SMARTi | View protein in SMART SM00220, S_TKc, 1 hit |
SUPFAMi | SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MSPRVGVTLS GRYRLQRLIA TGGMGQVWEA VDNRLGRRVA VKVLKSEFSS
60 70 80 90 100
DPEFIERFRA EARTTAMLNH PGIASVHDYG ESQMNGEGRT AYLVMELVNG
110 120 130 140 150
EPLNSVLKRT GRLSLRHALD MLEQTGRALQ IAHAAGLVHR DVKPGNILIT
160 170 180 190 200
PTGQVKITDF GIAKAVDAAP VTQTGMVMGT AQYIAPEQAL GHDASPASDV
210 220 230 240 250
YSLGVVGYEA VSGKRPFAGD GALTVAMKHI KEPPPPLPPD LPPNVRELIE
260 270 280 290 300
ITLVKNPAMR YRSGGPFADA VAAVRAGRRP PRPSQTPPPG RAAPAAIPSG
310 320 330 340 350
TTARVAANSA GRTAASRRSR PATGGHRPPR RTFSSGQRAL LWAAGVLGAL
360 370 380 390 400
AIIIAVLLVI KAPGDNSPQQ APTPTVTTTG NPPASNTGGT DASPRLNWTE
410 420 430
RGETRHSGLQ SWVVPPTPHS RASLARYEIA Q
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP42737.1 |
PIRi | E70699 |
RefSeqi | NP_214529.1, NC_000962.3 WP_003400358.1, NZ_KK339370.1 |
Genome annotation databases
GeneIDi | 45423974 885953 |
KEGGi | mtu:Rv0015c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP42737.1 |
PIRi | E70699 |
RefSeqi | NP_214529.1, NC_000962.3 WP_003400358.1, NZ_KK339370.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4OW8 | X-ray | 2.03 | A | 1-283 | [»] | |
4X3F | X-ray | 2.90 | A/B/C | 1-336 | [»] | |
6B2Q | X-ray | 2.88 | A/B/C/D | 1-296 | [»] | |
SMRi | P9WI83 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P9WI83, 2 interactors |
STRINGi | 83332.Rv0015c |
Chemistry databases
BindingDBi | P9WI83 |
ChEMBLi | CHEMBL4295585 |
PTM databases
iPTMneti | P9WI83 |
Proteomic databases
PaxDbi | P9WI83 |
Protocols and materials databases
DNASUi | 885953 |
Genome annotation databases
GeneIDi | 45423974 885953 |
KEGGi | mtu:Rv0015c |
Organism-specific databases
TubercuListi | Rv0015c |
Phylogenomic databases
eggNOGi | COG0515, Bacteria |
OMAi | CPGAPTT |
PhylomeDBi | P9WI83 |
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 3445 |
Family and domain databases
InterProi | View protein in InterPro IPR011009, Kinase-like_dom_sf IPR000719, Prot_kinase_dom IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF00069, Pkinase, 1 hit |
SMARTi | View protein in SMART SM00220, S_TKc, 1 hit |
SUPFAMi | SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PKNA_MYCTU | |
Accessioni | P9WI83Primary (citable) accession number: P9WI83 Secondary accession number(s): L0T594, P65726, P71585 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | February 23, 2022 | |
This is version 55 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families