P9WI69 · PKNI_MYCTU
- ProteinSerine/threonine-protein kinase PknI
- GenepknI
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids585 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays an important role in slowing down the growth of mycobacteria within the infected host (PubMed:19341393).
Activates the peroxidase activity of Rv2159c in a phosphorylation independent manner during oxidative stress conditions and thereby maintains the cellular homeostasis (PubMed:27818650).
Activates the peroxidase activity of Rv2159c in a phosphorylation independent manner during oxidative stress conditions and thereby maintains the cellular homeostasis (PubMed:27818650).
Miscellaneous
Several structural motifs known to be critical for the activity of eukaryotic-like Ser/Thr protein kinases (ePKs) are severely degraded in PknI (PubMed:28054744).
No kinase activity was detected by Lisa et al. for the catalytic domain of PknI, against different substrates and in various experimental conditions, suggesting that PknI may rely on unconventional mechanism(s) for kinase activity and/or it could play alternative role(s) in mycobacterial signaling (PubMed:28054744).
No kinase activity was detected by Lisa et al. for the catalytic domain of PknI, against different substrates and in various experimental conditions, suggesting that PknI may rely on unconventional mechanism(s) for kinase activity and/or it could play alternative role(s) in mycobacterial signaling (PubMed:28054744).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Activity regulation
Dimerization of the C-terminal extracellular sensor domain activates kinase autophosphorylation activity.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 18-26 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGCSAMGEV | ||||||
Binding site | 41 | ADP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 41 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 90 | ADP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92 | ADP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Active site | 137 | Proton acceptor | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | manganese ion binding | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | peptidyl-serine phosphorylation | |
Biological Process | peptidyl-threonine phosphorylation | |
Biological Process | protein autophosphorylation | |
Biological Process | regulation of growth rate |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase PknI
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionP9WI69
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Note: More abundant in the cytosol than in the cell membrane.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-349 | Cytoplasmic | ||||
Sequence: MALASGVTFAGYTVVRMLGCSAMGEVYLVQHPGFPGWQALKVLSPAMAADDEFRRRFQRETEVAARLFHPHILEVHDRGEFDGQLWIAMDYVDGIDATQHMADRFPAVLPVGEVLAIVTAVAGALDYAHQRGLLHRDVNPANVVLTSQSAGDQRILLADFGIASQPSYPAPELSAGADVDGRADQYALALTAIHLFAGAPPVDRSHTGPLQPPKLSAFRPDLARLDGVLSRALATAPADRFGSCREFADAMNEQAGVAIADQSSGGVDASEVTAAAGEEAYVVDYPAYGWPEAVDCKEPSARAPAPAAPTPQRRGSMLQSAAGVLARRLDNFSTATKAPASPTRRRPRR | ||||||
Transmembrane | 350-370 | Helical | ||||
Sequence: ILVGAVAVLLLAGLFAVGIVI | ||||||
Topological domain | 371-585 | Extracellular | ||||
Sequence: GRKTNTTATEVARPPTSGSAVPSAPTTTVAVTAPVPLDGTYRIEIQRSKQTYDYTPTPQPPDVNTWWAFRTSCTPTECLAAATMLDDNDHTQAKTPPVRPFLMQFGEGQWKSRPETVQFPCVGPNGSPSTQATTQLLALRPQPQGDLVGEMVVTVHSNECGQQGAVIRIPAVASRSGDLPPAVTVPDPATIPDTPDTTSTATLTPPTTTAPGPGR |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mutants show increased growth within macrophages and a hypervirulence phenotype in severe combined immunodeficiency mice.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 413 | Results in a conformational transition from dimer to monomer. | ||||
Sequence: I → E, K, or G | ||||||
Mutagenesis | 430 | Favors the presence of monomers in solution. | ||||
Sequence: P → G | ||||||
Mutagenesis | 431 | Favors the presence of monomers in solution. | ||||
Sequence: P → G |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000171220 | 1-585 | Serine/threonine-protein kinase PknI | |||
Sequence: MALASGVTFAGYTVVRMLGCSAMGEVYLVQHPGFPGWQALKVLSPAMAADDEFRRRFQRETEVAARLFHPHILEVHDRGEFDGQLWIAMDYVDGIDATQHMADRFPAVLPVGEVLAIVTAVAGALDYAHQRGLLHRDVNPANVVLTSQSAGDQRILLADFGIASQPSYPAPELSAGADVDGRADQYALALTAIHLFAGAPPVDRSHTGPLQPPKLSAFRPDLARLDGVLSRALATAPADRFGSCREFADAMNEQAGVAIADQSSGGVDASEVTAAAGEEAYVVDYPAYGWPEAVDCKEPSARAPAPAAPTPQRRGSMLQSAAGVLARRLDNFSTATKAPASPTRRRPRRILVGAVAVLLLAGLFAVGIVIGRKTNTTATEVARPPTSGSAVPSAPTTTVAVTAPVPLDGTYRIEIQRSKQTYDYTPTPQPPDVNTWWAFRTSCTPTECLAAATMLDDNDHTQAKTPPVRPFLMQFGEGQWKSRPETVQFPCVGPNGSPSTQATTQLLALRPQPQGDLVGEMVVTVHSNECGQQGAVIRIPAVASRSGDLPPAVTVPDPATIPDTPDTTSTATLTPPTTTAPGPGR |
Post-translational modification
Autophosphorylated at serine and threonine residues.
Proteomic databases
Expression
Induction
Expression decreases during infection of human macrophages.
Interaction
Subunit
Probably functions as a dimer in the regulation of M.tuberculosis growth (PubMed:28712808).
In the absence of stimuli, exists in a monomer-dimer equilibrium: a monomer form with no activity and a domain-swapped dimer form with a basic level of autophosphorylation activity (PubMed:28712808).
The presence of stimuli results in a shift in the monomer-dimer equilibrium, leading to the formation of more dimeric PknI (PubMed:28712808).
Specifically interacts with two peroxidase proteins, Rv2159c and Rv0148 (PubMed:26546727, PubMed:27818650).
The PknI-Rv2159c interaction is mediated through phosphorylation independent physical interaction (PubMed:27818650).
In the absence of stimuli, exists in a monomer-dimer equilibrium: a monomer form with no activity and a domain-swapped dimer form with a basic level of autophosphorylation activity (PubMed:28712808).
The presence of stimuli results in a shift in the monomer-dimer equilibrium, leading to the formation of more dimeric PknI (PubMed:28712808).
Specifically interacts with two peroxidase proteins, Rv2159c and Rv0148 (PubMed:26546727, PubMed:27818650).
The PknI-Rv2159c interaction is mediated through phosphorylation independent physical interaction (PubMed:27818650).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-252 | Protein kinase | ||||
Sequence: YTVVRMLGCSAMGEVYLVQHPGFPGWQALKVLSPAMAADDEFRRRFQRETEVAARLFHPHILEVHDRGEFDGQLWIAMDYVDGIDATQHMADRFPAVLPVGEVLAIVTAVAGALDYAHQRGLLHRDVNPANVVLTSQSAGDQRILLADFGIASQPSYPAPELSAGADVDGRADQYALALTAIHLFAGAPPVDRSHTGPLQPPKLSAFRPDLARLDGVLSRALATAPADRFGSCREFADAMN | ||||||
Region | 546-585 | Disordered | ||||
Sequence: SGDLPPAVTVPDPATIPDTPDTTSTATLTPPTTTAPGPGR | ||||||
Compositional bias | 561-579 | Polar residues | ||||
Sequence: IPDTPDTTSTATLTPPTTT |
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length585
- Mass (Da)61,805
- Last updated2014-04-16 v1
- ChecksumE52EACFF4A69C3EC
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 561-579 | Polar residues | ||||
Sequence: IPDTPDTTSTATLTPPTTT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL123456 EMBL· GenBank· DDBJ | CCP45716.1 EMBL· GenBank· DDBJ | Genomic DNA |