P9WI69 · PKNI_MYCTU

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).

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).

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Activity regulation

Dimerization of the C-terminal extracellular sensor domain activates kinase autophosphorylation activity.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site18-26ATP (UniProtKB | ChEBI)
Binding site41ADP (UniProtKB | ChEBI)
Binding site41ATP (UniProtKB | ChEBI)
Binding site90ADP (UniProtKB | ChEBI)
Binding site92ADP (UniProtKB | ChEBI)
Active site137Proton acceptor

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionmanganese ion binding
Molecular Functionprotein kinase activity
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processpeptidyl-serine phosphorylation
Biological Processpeptidyl-threonine phosphorylation
Biological Processprotein autophosphorylation
Biological Processregulation of growth rate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein kinase PknI
  • EC number

Gene names

    • Name
      pknI
    • ORF names
      MTCY338.02c
    • Ordered locus names
      Rv2914c

Organism names

Accessions

  • Primary accession
    P9WI69
  • Secondary accessions
    • L0TB90
    • P65730
    • Q10964

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Cell membrane
; Single-pass membrane protein
Note: More abundant in the cytosol than in the cell membrane.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-349Cytoplasmic
Transmembrane350-370Helical
Topological domain371-585Extracellular

Keywords

Phenotypes & Variants

Disruption phenotype

Mutants show increased growth within macrophages and a hypervirulence phenotype in severe combined immunodeficiency mice.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis413Results in a conformational transition from dimer to monomer.
Mutagenesis430Favors the presence of monomers in solution.
Mutagenesis431Favors the presence of monomers in solution.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001712201-585Serine/threonine-protein kinase PknI

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).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain12-252Protein kinase
Region546-585Disordered
Compositional bias561-579Polar residues

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    585
  • Mass (Da)
    61,805
  • Last updated
    2014-04-16 v1
  • Checksum
    E52EACFF4A69C3EC
MALASGVTFAGYTVVRMLGCSAMGEVYLVQHPGFPGWQALKVLSPAMAADDEFRRRFQRETEVAARLFHPHILEVHDRGEFDGQLWIAMDYVDGIDATQHMADRFPAVLPVGEVLAIVTAVAGALDYAHQRGLLHRDVNPANVVLTSQSAGDQRILLADFGIASQPSYPAPELSAGADVDGRADQYALALTAIHLFAGAPPVDRSHTGPLQPPKLSAFRPDLARLDGVLSRALATAPADRFGSCREFADAMNEQAGVAIADQSSGGVDASEVTAAAGEEAYVVDYPAYGWPEAVDCKEPSARAPAPAAPTPQRRGSMLQSAAGVLARRLDNFSTATKAPASPTRRRPRRILVGAVAVLLLAGLFAVGIVIGRKTNTTATEVARPPTSGSAVPSAPTTTVAVTAPVPLDGTYRIEIQRSKQTYDYTPTPQPPDVNTWWAFRTSCTPTECLAAATMLDDNDHTQAKTPPVRPFLMQFGEGQWKSRPETVQFPCVGPNGSPSTQATTQLLALRPQPQGDLVGEMVVTVHSNECGQQGAVIRIPAVASRSGDLPPAVTVPDPATIPDTPDTTSTATLTPPTTTAPGPGR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias561-579Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL123456
EMBL· GenBank· DDBJ
CCP45716.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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