Protein Variants | Comment | Organism |
---|---|---|
additional information | creating a conditional gene replacement pstP mutant in Mycobacterium smegmatis, using the recombineering method, depletion of PstP in Mycobacterium smegmatis leads to cell death/poor cell survival, phenotype, overview | Mycolicibacterium smegmatis |
additional information | overexpression and conditional gene replacement of pstP with depletion of PstP in Mycobacterium tuberculosis, phenotypes, overview | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
[protein]-serine/threonine phosphate + H2O | Mycolicibacterium smegmatis | - |
[protein]-serine/threonine + phosphate | - |
? | |
[protein]-serine/threonine phosphate + H2O | Mycobacterium tuberculosis | - |
[protein]-serine/threonine + phosphate | - |
? | |
[protein]-serine/threonine phosphate + H2O | Mycobacterium tuberculosis H37Rv | - |
[protein]-serine/threonine + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WHW5 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WHW5 | - |
- |
Mycolicibacterium smegmatis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
[protein]-serine/threonine phosphate + H2O | - |
Mycolicibacterium smegmatis | [protein]-serine/threonine + phosphate | - |
? | |
[protein]-serine/threonine phosphate + H2O | - |
Mycobacterium tuberculosis | [protein]-serine/threonine + phosphate | - |
? | |
[protein]-serine/threonine phosphate + H2O | - |
Mycobacterium tuberculosis H37Rv | [protein]-serine/threonine + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | domain structure overview | Mycolicibacterium smegmatis |
More | domain structure overview | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
PSTP | - |
Mycolicibacterium smegmatis |
PSTP | - |
Mycobacterium tuberculosis |
Rv0018c | - |
Mycobacterium tuberculosis |
serine/threonine protein phosphatase | - |
Mycolicibacterium smegmatis |
serine/threonine protein phosphatase | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
malfunction | overexpression of PstP leads to elongated cells and partially compromised survival. Depletion of PstP in Mycobacterium smegmatis leads to cell death | Mycolicibacterium smegmatis |
malfunction | overexpression of PstP leads to elongated cells and partially compromised survival. Depletion of PstP is detrimental to cell survival, eventually leading to cell death. PstP depletion results in elongated multiseptate cells, suggesting a role for PstP in regulating cell division events. Depletion of PstP decreases the bacillary load even in an established infection. Marginally compromised survival in complementation experiments. All of the domains, including the extracellular domain, are necessary for complete rescue. Depletion of PstP from established infections causes pathogen clearance, indicating that the continued presence of PstP is necessary for pathogen survival | Mycobacterium tuberculosis |
physiological function | serine/threonine protein phosphatase PstP of Mycobacterium tuberculosis is necessary for accurate cell division and survival of pathogen, role for PstP in regulating cell division events. The activity of PstP is essential for mycobacterial growth. All of the enzyme domains, including the extracellular domain, are necessary for enzyme activity in vivo. The catalytic activity of PstP is absolutely essential for the in vitro growth | Mycolicibacterium smegmatis |
physiological function | serine/threonine protein phosphatase PstP of Mycobacterium tuberculosis is necessary for accurate cell division and survival of pathogen, role for PstP in regulating cell division events. The activity of PstP is essential for mycobacterial growth. All of the enzyme domains, including the extracellular domain, are necessary for enzyme activity in vivo. The catalytic activity of PstP is absolutely essential for the in vitro growth | Mycobacterium tuberculosis |