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Literature summary extracted from
- Mycobacterial serine/threonine phosphatase PstP is phosphoregulated and localized to mediate control of cell wall metabolism (2022), Mol. Microbiol., 118, 47-60.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.3.16 | additional information | construction of Msmeg strains with a phospho-mimetic pstPT134EMsmeg allele and a phospho-ablative pstPT134AMsmeg allele replacing the wild-type pstP | Mycolicibacterium smegmatis |
| 3.1.3.16 | T134A | site-directed mutagenesis, phospho-mimetic mutation of T134 on PstP. PstPT134AMsmeg is not stable | Mycolicibacterium smegmatis |
| 3.1.3.16 | T134E | naturally occurring mutation, phospho-mimetic mutation of T134 on PstP. PstPT134EMsmeg is stable. The mutation in Mycobacterium smegmatis (Msmeg) causes misregulation of peptidoglycan in vivo. The mutant strain has inconsistent doubling times | Mycolicibacterium smegmatis |
| 3.1.3.16 | T137E | naturally occurring mutation, the phospho-mimetic mutation of T137 on PstP negatively regulates its catalytic activity against the cell wall regulators FhaA, Wag31, CwlM, PknB and PknA. His-tagged mutant PstPcT137EMtb is inactive in vitro against all tested substrates, except for His-/MBP-tagged PknBMtb and His-/MBP-tagged PknAMtb, but activity with the latter is reduced compared to wild-type | Mycobacterium tuberculosis |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.1.3.16 | cell septum | PstP is localized to the septum | Mycobacterium tuberculosis | 30428 | - |
| 3.1.3.16 | cell septum | PstP is localized to the septum | Mycolicibacterium smegmatis | 30428 | - |
| 3.1.3.16 | cell wall | - |
Mycobacterium tuberculosis | 5618 | - |
| 3.1.3.16 | cell wall | - |
Mycolicibacterium smegmatis | 5618 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.16 | additional information | the enzyme is dependent on divalent cation | Mycobacterium tuberculosis | |
| 3.1.3.16 | additional information | the enzyme is dependent on divalent cation | Mycolicibacterium smegmatis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.16 | Mycobacterium tuberculosis | P9WHW5 | - |
- |
| 3.1.3.16 | Mycobacterium tuberculosis ATCC 25618 | P9WHW5 | - |
- |
| 3.1.3.16 | Mycobacterium tuberculosis H37Rv | P9WHW5 | - |
- |
| 3.1.3.16 | Mycolicibacterium smegmatis | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.1.3.16 | phosphoprotein | PstPMtb is itself phosphorylated on T137, T141, T174 and T290. Phosphorylation on all these sites together affects PstP activity against small molecule substrates in vitro. Phosphorylation on T174 affects cell wall metabolism in vivo. Phosphorylation on T137 of PstP may in vivo inhibit its activity against multiple substrates | Mycobacterium tuberculosis |
| 3.1.3.16 | phosphoprotein | phosphorylation on T174 affects cell wall metabolism in vivo in Mycobacterium smegmatis | Mycolicibacterium smegmatis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.16 | [CwlM]-serine/threonine phosphate + H2O | in vitro substrate His-/SUMO-tagged CwlMMtb | Mycobacterium tuberculosis | [CwlM]-serine/threonine + phosphate | - |
? |  |
| 3.1.3.16 | [CwlM]-serine/threonine phosphate + H2O | in vitro substrate His-/SUMO-tagged CwlMMtb | Mycolicibacterium smegmatis | [CwlM]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [CwlM]-serine/threonine phosphate + H2O | in vitro substrate His-/SUMO-tagged CwlMMtb | Mycobacterium tuberculosis H37Rv | [CwlM]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [CwlM]-serine/threonine phosphate + H2O | in vitro substrate His-/SUMO-tagged CwlMMtb | Mycobacterium tuberculosis ATCC 25618 | [CwlM]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [FhaA]-serine/threonine phosphate + H2O | in vitro substrate His-tagged FhaAMtb | Mycobacterium tuberculosis | [FhaA]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [FhaA]-serine/threonine phosphate + H2O | in vitro substrate His-tagged FhaAMtb | Mycolicibacterium smegmatis | [FhaA]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [FhaA]-serine/threonine phosphate + H2O | in vitro substrate His-tagged FhaAMtb | Mycobacterium tuberculosis H37Rv | [FhaA]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [FhaA]-serine/threonine phosphate + H2O | in vitro substrate His-tagged FhaAMtb | Mycobacterium tuberculosis ATCC 25618 | [FhaA]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [PknA]-serine/threonine phosphate + H2O | - |
Mycobacterium tuberculosis | [PknA]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [PknA]-serine/threonine phosphate + H2O | - |
Mycolicibacterium smegmatis | [PknA]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [PknA]-serine/threonine phosphate + H2O | - |
Mycobacterium tuberculosis H37Rv | [PknA]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [PknA]-serine/threonine phosphate + H2O | - |
Mycobacterium tuberculosis ATCC 25618 | [PknA]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [PknB]-serine/threonine phosphate + H2O | - |
Mycobacterium tuberculosis | [PknB]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [PknB]-serine/threonine phosphate + H2O | - |
Mycolicibacterium smegmatis | [PknB]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [PknB]-serine/threonine phosphate + H2O | - |
Mycobacterium tuberculosis H37Rv | [PknB]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [PknB]-serine/threonine phosphate + H2O | - |
Mycobacterium tuberculosis ATCC 25618 | [PknB]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [Wag31]-serine/threonine phosphate + H2O | in vitro substrate His-tagged Wag31Mtb | Mycobacterium tuberculosis | [Wag31]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [Wag31]-serine/threonine phosphate + H2O | in vitro substrate His-tagged Wag31Mtb | Mycolicibacterium smegmatis | [Wag31]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [Wag31]-serine/threonine phosphate + H2O | in vitro substrate His-tagged Wag31Mtb | Mycobacterium tuberculosis H37Rv | [Wag31]-serine/threonine + phosphate | - |
? | |
| 3.1.3.16 | [Wag31]-serine/threonine phosphate + H2O | in vitro substrate His-tagged Wag31Mtb | Mycobacterium tuberculosis ATCC 25618 | [Wag31]-serine/threonine + phosphate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.16 | PSTP | - |
Mycobacterium tuberculosis |
| 3.1.3.16 | PSTP | - |
Mycolicibacterium smegmatis |
| 3.1.3.16 | serine/threonine phosphatase | - |
Mycobacterium tuberculosis |
| 3.1.3.16 | serine/threonine phosphatase | - |
Mycolicibacterium smegmatis |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.3.16 | evolution | enzyme PstP belongs to the protein phosphatase 2C (PP2C) subfamily of divalent metal-ion dependent protein serine/threonine phosphatases | Mycobacterium tuberculosis |
| 3.1.3.16 | evolution | enzyme PstP belongs to the protein phosphatase 2C (PP2C) subfamily of divalent metal-ion dependent protein serine/threonine phosphatases | Mycolicibacterium smegmatis |
| 3.1.3.16 | malfunction | a phospho-mimetic mutation of T137 on PstP negatively regulates its catalytic activity against the cell wall regulators FhaA, Wag31, CwlM, PknB and PknA. The His-tagged mutant PstPcT137EMtb is inactive in vitro against all tested substrates, except for His-/MBP-tagged PknBMtb and His-/MBP-tagged PknAMtb, but activity with the latter is reduced compared to wild-type | Mycobacterium tuberculosis |
| 3.1.3.16 | malfunction | phosphorylation on T174 affects cell wall metabolism in vivo in Mycobacterium smegmatis. The mutation T134E/A in Mycobacterium smegmatis (Msmeg) causes misregulation of peptidoglycan in vivo | Mycolicibacterium smegmatis |
| 3.1.3.16 | metabolism | PstP belongs to the protein phosphatase 2C (PP2C) subfamily of divalent metal-ion dependent protein serine/threonine phosphatases, which regulate prokaryotic and eukaryotic cell growth and division, sporulation, stress response and metabolic processes in response to various environmental signals. The regulation of PstP is involved in the control of cell wall metabolism in mycobacteria. A negative charge on T134 of PstPMsmeg regulates peptidoglycan metabolism in starvation | Mycobacterium tuberculosis |
| 3.1.3.16 | metabolism | PstP belongs to the protein phosphatase 2C (PP2C) subfamily of divalent metal-ion dependent protein serine/threonine phosphatases, which regulate prokaryotic and eukaryotic cell growth and division, sporulation, stress response and metabolic processes in response to various environmental signals. The regulation of PstP is involved in the control of cell wall metabolism in mycobacteria. A negative charge on T134 of PstPMsmeg regulates peptidoglycan metabolism in starvation | Mycolicibacterium smegmatis |
| 3.1.3.16 | physiological function | PstP is the only mycobacterial S/T protein phosphatase. PstP dephosphorylates two regulators of peptidoglycan in Mtb, FhaA and Wag31. FhaA and Wag31 are both regulators of mycobacterial cell wall metabolism | Mycobacterium tuberculosis |
| 3.1.3.16 | physiological function | PstP is the only mycobacterial S/T protein phosphatase. PstP is essential in Mycobacterium smegmatis. A negative charge on T134 of PstPMsmeg regulates peptidoglycan metabolism in starvation | Mycolicibacterium smegmatis |
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