P9WI78 · PKND_MYCTO

Function

function

Part of a signaling pathway that enables adaptation to osmotic stress through cell wall remodeling and virulence factor production.
Key microbial factor required for central nervous system tuberculosis. Required for invasion of host brain endothelia, but not macrophages, lung epithelia or other endothelia.

Catalytic activity

Activity regulation

Dimerization activates the kinase domain of unphosphorylated PknD via an allosteric mechanism, triggering autophosphorylation and phosphorylation of target proteins. Phosphorylated PknD is fully active even in the absence of dimerization.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site21-29ATP (UniProtKB | ChEBI)
Binding site44ATP (UniProtKB | ChEBI)
Active site138Proton acceptor

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processregulation of primary metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      pknD
    • Ordered locus names
      MT0958

Organism names

Accessions

  • Primary accession
    P9WI78
  • Secondary accessions
    • L0T6U6
    • O05871
    • P95308

Proteomes

Subcellular Location

Cell membrane
; Single-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-381Cytoplasmic
Transmembrane382-402Helical
Topological domain403-664Extracellular

Keywords

Phenotypes & Variants

Disruption phenotype

Mutants display defective invasion and reduced survival in brain endothelia.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004280541-664Serine/threonine-protein kinase PknD
Modified residue135Phosphothreonine; by autocatalysis
Modified residue169Phosphothreonine; by autocatalysis
Modified residue171Phosphothreonine; by autocatalysis
Modified residue173Phosphothreonine; by autocatalysis
Modified residue209Phosphothreonine; by autocatalysis

Post-translational modification

Autophosphorylated. Dephosphorylated by PstP.

Keywords

Interaction

Subunit

Homodimer (By similarity).
The extracellular domain interacts with host laminin (PubMed:22243650).

Structure

Family & Domains

Features

Showing features for domain, region, repeat.

TypeIDPosition(s)Description
Domain15-276Protein kinase
Region303-333Disordered
Repeat414-456NHL 1
Repeat457-497NHL 2
Repeat498-539NHL 3
Repeat540-581NHL 4
Repeat582-623NHL 5
Repeat624-664NHL 6

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
    664
  • Mass (Da)
    69,545
  • Last updated
    2014-04-16 v1
  • Checksum
    FE39716825A41CC1
MSDAVPQVGSQFGPYQLLRLLGRGGMGEVYEAEDTRKHRVVALKLISPQYSDNAVFRARMQREADTAGRLTEPHIVPIHDYGEINGQFFVEMRMIDGTSLRALLKQYGPLTPARAVAIVRQIAAALDAAHANGVTHRDVKPENILVTASDFAYLVDFGIARAASDPGLTQTGTAVGTYNYMAPERFTGDEVTYRADIYALACVLGECLTGAPPYRADSVERLIAAHLMDPAPQPSQLRPGRVPPALDQVIAKGMAKNPAERFMSAGDLAIAAHDALTTSEQHQATTILRRGDNATLLATPADTGLSQSESGIAGAGTGPPTPGAARWSPGDSATVAGPLAADSRGGNWPSQTGHSPAVPNALQASLGHAVPPAGNKRKVWAVVGAAAIVLVAIVAAAGYLVLRPSWSPTQASGQTVLPFTGIDFRLSPSGVAVDSAGNVYVTSEGMYGRVVKLATGSTGTTVLPFNGLYQPQGLAVDGAGTVYVTDFNNRVVTLAAGSNNQTVLPFDGLNYPEGLAVDTQGAVYVADRGNNRVVKLAAGSKTQTVLPFTGLNDPDGVAVDNSGNVYVTDTDNNRVVKLEAESNNQVVLPFTDITAPWGIAVDEAGTVYVTEHNTNQVVKLLAGSTTSTVLPFTGLNTPLAVAVDSDRTVYVADRGNDRVVKLTS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE000516
EMBL· GenBank· DDBJ
AAK45205.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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