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UniProt functional annotation for P9WI79 | ||
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| UniProt code: P9WI79. |
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| Organism: | |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). |
| Taxonomy: | |
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex. |
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| Function: | |
Part of a signaling pathway that enables adaptation to osmotic stress through cell wall remodeling and virulence factor production (PubMed:24309377). Phosphorylates the osmosensory protein OprA, which inhibits binding of OprA to Rv2638, leading to the regulation of osmotically regulated genes, including the ESX-1- associated virulence factor espA (PubMed:17411339, PubMed:17242402, PubMed:24309377). In addition, directly phosphorylates the alternative sigma factor SigF and its regulator, Rv1364c, which regulates the SigF- Rv1364c interaction (PubMed:30642988). Can also phosphorylate the FHA domain of Rv1747 (PubMed:15987910). {ECO:0000269|PubMed:15987910, ECO:0000269|PubMed:17242402, ECO:0000269|PubMed:17411339, ECO:0000269|PubMed:24309377, ECO:0000269|PubMed:30642988}. |
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| Function: | |
Key microbial factor required for central nervous system tuberculosis. Required for invasion of host brain endothelia, but not macrophages, lung epithelia or other endothelia. {ECO:0000250|UniProtKB:P9WI78}. |
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| Catalytic activity: | |
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:17242402, ECO:0000269|PubMed:17411339, ECO:0000269|PubMed:30642988}; |
| Catalytic activity: | |
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:17242402, ECO:0000269|PubMed:17411339, ECO:0000269|PubMed:24309377, ECO:0000269|PubMed:30642988}; |
| 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. {ECO:0000269|PubMed:17242402}. |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:17242402}. |
| Subcellular location: | |
Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. |
| Induction: | |
Increased expression after 3 hours of phosphate starvation, no protein detected after 24 hours phosphate starvation (at protein level). Part of the pstS2-pknD operon. {ECO:0000269|PubMed:20933472}. |
| Ptm: | |
Autophosphorylated (PubMed:15967413, PubMed:16739134, PubMed:17242402). Dephosphorylated by PstP (PubMed:15967413). {ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:16739134, ECO:0000269|PubMed:17242402}. |
| Disruption phenotype: | |
No growth phenotype in phosphate-rich medium (3.6 mM Pi), in restricted medium (Sauton) grows better than wild-type but in phosphate-free Sauton medium dies faster than wild-type when pre- exposed to starvation. {ECO:0000269|PubMed:20933472}. |
| Similarity: | |
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. |
Annotations taken from UniProtKB at the EBI.