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MYCTU:PKNA
Contents
| Species (Taxon ID) | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332) | |
| Gene Name(s) | pknA | |
| Protein Name(s) | Serine/threonine-protein kinase PknA | |
| External Links | ||
| UniProt | P9WI83 | |
| EMBL | AL123456 | |
| PIR | E70699 | |
| RefSeq | NP_214529.1 WP_003400358.1 | |
| PDB | 4OW8 4X3F | |
| PDBsum | 4OW8 4X3F | |
| ProteinModelPortal | P9WI83 | |
| SMR | P9WI83 | |
| IntAct | P9WI83 | |
| STRING | 83332.Rv0015c | |
| iPTMnet | P9WI83 | |
| PaxDb | P9WI83 | |
| EnsemblBacteria | CCP42737 | |
| GeneID | 885953 | |
| KEGG | mtu:Rv0015c | |
| TubercuList | Rv0015c | |
| eggNOG | ENOG4107TPY COG0515 | |
| KO | K12132 | |
| OMA | FVERFRI | |
| PhylomeDB | P9WI83 | |
| Proteomes | UP000001584 | |
| GO | GO:0005829 GO:0005576 GO:0016021 GO:0005886 GO:0005524 GO:0004672 GO:0004674 GO:0040007 GO:0043086 GO:0045717 GO:0051055 GO:0009405 GO:0043085 GO:0043388 GO:0046777 GO:0006468 GO:0008360 | |
| InterPro | IPR011009 IPR000719 IPR008271 | |
| Pfam | PF00069 | |
| SMART | SM00220 | |
| SUPFAM | SSF56112 | |
| PROSITE | PS50011 PS00108 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0009405 |
pathogenesis |
ECO:0000315 |
P |
Figure 5A: The lungs of the animals infected with the wild type Mycobacterium tuberculosis H37Rv and the complemented (containing pknA and pknB placed at the L5 site on the chromosome) strain showed an immense infection and large granulomas where the deleted pknA mutant showed normal lung observation. Figure 5B: looked at lesions in the lungs, showing that the wild type infection caused more damage when compared to the complemented strain. Figure 5c: A histopathological analysis revealed less severe damage in the complemented strain when compared to the wild type strain. |
complete | |||||
| GO:1990443 |
peptidyl-threonine autophosphorylation |
ECO:0000315 |
P |
Fig 9(b + d): The protein phosphokinase A (pknA) was detected in a wild strain Mycobacterium tuberculosis H37Rv using the antibody alpha-Thr(P), which picks up the threonine residues 172 and 174 in the pkna activation loop. PknA was not detected in the strain pknA(K42M), a strain where kinases were inactivated. This suggested that kinases (like pknA) were being activated by auto-phosphorylation. Fig 9e: In a strain in which the transcription level of pknB is under the control of a pristinamycin inducible promoter, the level of pknA is not impacted whether the strain is grown in the presence or absence of the inducer. This is indicative that pknA is most likely activated through auto-phosphorylation and is independent of pknB |
complete | |||||
| GO:0044117 |
growth of symbiont in host |
ECO:0000315 |
P |
Figure 4B: Graph shows similar cfu counts for the wild type Mycobacterium tuberculosis H37Rv, the complemented (pknA and pknB) strain, and pknB strain at 24 hours. The wild type and complemented strain expressed increased growth at both 4 and 8 weeks while the cfu counts for the pknB strain was below the detection range at both 4 and 8 weeks post infection. Figure 6C: Shows a growth analysis through absorbance readings over the course of three hours where the pknA strain grew and the pknA mutant showed no growth nor growth recovery. Figure 6D: When plated on ATc (anhydrotetracycline) plates without pristinamycin the complemented strain grew while the pknA mutant and pknB strain did not grow. |
complete | |||||
| GO:0008360 |
regulation of cell shape |
ECO:0000315 |
P |
Mycobacterium tuberculosis (strain H37Rv) Serine/threonine-protein kinase A Figure 3B: The cell morphologies of Mycobacterium tuberculosis strains H37Rv (wild-type), Rv-pptr-AB (pknA and pknB conditional mutant, pknA-pknB expression was under the regulation of a pristinamycin inducible promoter [pptr]), and Rv-pptr-AB::PknB (electroporated with pCiT-PknB, containing anhydrotetracycline [ATc] inducible PknB) were examined using scanning electron microscopy. H37Rv cultures were grown for 4 days in the absence of any inducer. Rv-pptr-AB cultures were grown either in the presence or absence of pristinamycin for 2 and 4 days. Rv-pptr-AB::PknB cultures were grown in the presence of ATc (in the absence of pristinamycin) for 2 and 4 days. After 4 days of growth, Rv-pptr-AB and Rv-pptr-AB::PknB cells showed signs of substantial cell-cell fusion and cell lysis, relative to the wild-type H37Rv. These results suggest that PknA plays a role in regulating cell morphology in Mycobacterium tuberculosis. |
complete | |||||
|
involved_in |
GO:0043086 |
negative regulation of catalytic activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0043085 |
positive regulation of catalytic activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005576 |
extracellular region |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004672 |
protein kinase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0051055 |
negative regulation of lipid biosynthetic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0046777 |
protein autophosphorylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0046777 |
protein autophosphorylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0046777 |
protein autophosphorylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0045717 |
negative regulation of fatty acid biosynthetic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0043388 |
positive regulation of DNA binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0043086 |
negative regulation of catalytic activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0008360 |
regulation of cell shape |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0008360 |
regulation of cell shape |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006468 |
protein phosphorylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004674 |
protein serine/threonine kinase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004672 |
protein kinase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004672 |
protein kinase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004672 |
protein kinase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004672 |
protein kinase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004672 |
protein kinase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004672 |
protein kinase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004672 |
protein kinase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006468 |
protein phosphorylation |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016301 |
kinase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016021 |
integral component of membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0016310 |
phosphorylation |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009405 |
pathogenesis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004674 |
protein serine/threonine kinase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016740 |
transferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 1.3 Nagarajan, SN et al. (2015) Protein kinase A (PknA) of Mycobacterium tuberculosis is independently activated and is critical for growth in vitro and survival of the pathogen in the host. J. Biol. Chem. 290 9626-45 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 Molle, V et al. (2006) The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation. J. Biol. Chem. 281 30094-103 PubMed GONUTS page
- ↑ Mawuenyega, KG et al. (2005) Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Mol. Biol. Cell 16 396-404 PubMed GONUTS page
- ↑ Målen, H et al. (2007) Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics 7 1702-18 PubMed GONUTS page
- ↑ 5.0 5.1 Veyron-Churlet, R et al. (2009) The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue. J. Biol. Chem. 284 6414-24 PubMed GONUTS page
- ↑ 6.0 6.1 6.2 Singh, A et al. (2006) Protein kinase I of Mycobacterium tuberculosis: cellular localization and expression during infection of macrophage-like cells. Tuberculosis (Edinb) 86 28-33 PubMed GONUTS page
- ↑ 7.0 7.1 7.2 Kang, CM et al. (2005) The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape. Genes Dev. 19 1692-704 PubMed GONUTS page
- ↑ 8.0 8.1 8.2 Chaba, R et al. (2002) Evidence that a eukaryotic-type serine/threonine protein kinase from Mycobacterium tuberculosis regulates morphological changes associated with cell division. Eur. J. Biochem. 269 1078-85 PubMed GONUTS page
- ↑ Veyron-Churlet, R et al. (2010) Phosphorylation of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis. J. Biol. Chem. 285 12714-25 PubMed GONUTS page
- ↑ 10.0 10.1 Sharma, K et al. (2006) EmbR, a regulatory protein with ATPase activity, is a substrate of multiple serine/threonine kinases and phosphatase in Mycobacterium tuberculosis. FEBS J. 273 2711-21 PubMed GONUTS page
- ↑ 11.0 11.1 Thakur, M & Chakraborti, PK (2006) GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA. J. Biol. Chem. 281 40107-13 PubMed GONUTS page
- ↑ Sureka, K et al. (2010) Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division. PLoS ONE 5 e8590 PubMed GONUTS page
- ↑ Thakur, M & Chakraborti, PK (2008) Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis. Biochem. J. 415 27-33 PubMed GONUTS page
b
m
n
p
- GO:1990443 ! peptidyl-threonine autophosphorylation
- GO:0016310 ! phosphorylation
- GO:0005886 ! plasma membrane
- GO:0043388 ! positive regulation of DNA binding
- GO:0043085 ! positive regulation of catalytic activity
- GO:0046777 ! protein autophosphorylation
- GO:0004672 ! protein kinase activity
- GO:0006468 ! protein phosphorylation
- GO:0004674 ! protein serine/threonine kinase activity
