P9WI78 · PKND_MYCTO
- ProteinSerine/threonine-protein kinase PknD
- GenepknD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids664 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | regulation of primary metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase PknD
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionP9WI78
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-381 | Cytoplasmic | ||||
Sequence: MSDAVPQVGSQFGPYQLLRLLGRGGMGEVYEAEDTRKHRVVALKLISPQYSDNAVFRARMQREADTAGRLTEPHIVPIHDYGEINGQFFVEMRMIDGTSLRALLKQYGPLTPARAVAIVRQIAAALDAAHANGVTHRDVKPENILVTASDFAYLVDFGIARAASDPGLTQTGTAVGTYNYMAPERFTGDEVTYRADIYALACVLGECLTGAPPYRADSVERLIAAHLMDPAPQPSQLRPGRVPPALDQVIAKGMAKNPAERFMSAGDLAIAAHDALTTSEQHQATTILRRGDNATLLATPADTGLSQSESGIAGAGTGPPTPGAARWSPGDSATVAGPLAADSRGGNWPSQTGHSPAVPNALQASLGHAVPPAGNKRKVWA | ||||||
Transmembrane | 382-402 | Helical | ||||
Sequence: VVGAAAIVLVAIVAAAGYLVL | ||||||
Topological domain | 403-664 | Extracellular | ||||
Sequence: RPSWSPTQASGQTVLPFTGIDFRLSPSGVAVDSAGNVYVTSEGMYGRVVKLATGSTGTTVLPFNGLYQPQGLAVDGAGTVYVTDFNNRVVTLAAGSNNQTVLPFDGLNYPEGLAVDTQGAVYVADRGNNRVVKLAAGSKTQTVLPFTGLNDPDGVAVDNSGNVYVTDTDNNRVVKLEAESNNQVVLPFTDITAPWGIAVDEAGTVYVTEHNTNQVVKLLAGSTTSTVLPFTGLNTPLAVAVDSDRTVYVADRGNDRVVKLTS |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mutants display defective invasion and reduced survival in brain endothelia.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000428054 | 1-664 | Serine/threonine-protein kinase PknD | |||
Sequence: MSDAVPQVGSQFGPYQLLRLLGRGGMGEVYEAEDTRKHRVVALKLISPQYSDNAVFRARMQREADTAGRLTEPHIVPIHDYGEINGQFFVEMRMIDGTSLRALLKQYGPLTPARAVAIVRQIAAALDAAHANGVTHRDVKPENILVTASDFAYLVDFGIARAASDPGLTQTGTAVGTYNYMAPERFTGDEVTYRADIYALACVLGECLTGAPPYRADSVERLIAAHLMDPAPQPSQLRPGRVPPALDQVIAKGMAKNPAERFMSAGDLAIAAHDALTTSEQHQATTILRRGDNATLLATPADTGLSQSESGIAGAGTGPPTPGAARWSPGDSATVAGPLAADSRGGNWPSQTGHSPAVPNALQASLGHAVPPAGNKRKVWAVVGAAAIVLVAIVAAAGYLVLRPSWSPTQASGQTVLPFTGIDFRLSPSGVAVDSAGNVYVTSEGMYGRVVKLATGSTGTTVLPFNGLYQPQGLAVDGAGTVYVTDFNNRVVTLAAGSNNQTVLPFDGLNYPEGLAVDTQGAVYVADRGNNRVVKLAAGSKTQTVLPFTGLNDPDGVAVDNSGNVYVTDTDNNRVVKLEAESNNQVVLPFTDITAPWGIAVDEAGTVYVTEHNTNQVVKLLAGSTTSTVLPFTGLNTPLAVAVDSDRTVYVADRGNDRVVKLTS | ||||||
Modified residue | 135 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 169 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 171 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 173 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 209 | Phosphothreonine; by autocatalysis | ||||
Sequence: T |
Post-translational modification
Autophosphorylated. Dephosphorylated by PstP.
Keywords
- PTM
Interaction
Subunit
Homodimer (By similarity).
The extracellular domain interacts with host laminin (PubMed:22243650).
The extracellular domain interacts with host laminin (PubMed:22243650).
Structure
Family & Domains
Features
Showing features for domain, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 15-276 | Protein kinase | ||||
Sequence: YQLLRLLGRGGMGEVYEAEDTRKHRVVALKLISPQYSDNAVFRARMQREADTAGRLTEPHIVPIHDYGEINGQFFVEMRMIDGTSLRALLKQYGPLTPARAVAIVRQIAAALDAAHANGVTHRDVKPENILVTASDFAYLVDFGIARAASDPGLTQTGTAVGTYNYMAPERFTGDEVTYRADIYALACVLGECLTGAPPYRADSVERLIAAHLMDPAPQPSQLRPGRVPPALDQVIAKGMAKNPAERFMSAGDLAIAAHDAL | ||||||
Region | 303-333 | Disordered | ||||
Sequence: TGLSQSESGIAGAGTGPPTPGAARWSPGDSA | ||||||
Repeat | 414-456 | NHL 1 | ||||
Sequence: QTVLPFTGIDFRLSPSGVAVDSAGNVYVTSEGMYGRVVKLATG | ||||||
Repeat | 457-497 | NHL 2 | ||||
Sequence: STGTTVLPFNGLYQPQGLAVDGAGTVYVTDFNNRVVTLAAG | ||||||
Repeat | 498-539 | NHL 3 | ||||
Sequence: SNNQTVLPFDGLNYPEGLAVDTQGAVYVADRGNNRVVKLAAG | ||||||
Repeat | 540-581 | NHL 4 | ||||
Sequence: SKTQTVLPFTGLNDPDGVAVDNSGNVYVTDTDNNRVVKLEAE | ||||||
Repeat | 582-623 | NHL 5 | ||||
Sequence: SNNQVVLPFTDITAPWGIAVDEAGTVYVTEHNTNQVVKLLAG | ||||||
Repeat | 624-664 | NHL 6 | ||||
Sequence: STTSTVLPFTGLNTPLAVAVDSDRTVYVADRGNDRVVKLTS |
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length664
- Mass (Da)69,545
- Last updated2014-04-16 v1
- ChecksumFE39716825A41CC1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE000516 EMBL· GenBank· DDBJ | AAK45205.1 EMBL· GenBank· DDBJ | Genomic DNA |