UniProt functional annotation for P9WLZ7



	UniProt functional annotation for P9WLZ7

UniProt code: P9WLZ7.

Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).

Taxonomy: Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.

Function: Primarily acts as an independent SigF regulator that is sensitive to the osmosensory signal, mediating the cross talk of PknD with the SigF regulon (PubMed:30642988). Possesses both phosphatase and kinase activities (PubMed:30642988, PubMed:19700407). The kinase domain functions as a classic anti-sigma factor-like kinase to phosphorylate the anti-anti-sigma factor domain at the canonical regulatory site, and the phosphatase domain antagonizes this activity (PubMed:19700407). {ECO:0000269|PubMed:19700407, ECO:0000269|PubMed:30642988}.

Catalytic activity: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000255|PROSITE- ProRule:PRU01082, ECO:0000269|PubMed:19700407, ECO:0000269|PubMed:30642988};

Catalytic activity: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000255|PROSITE- ProRule:PRU01082};

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:19700407, 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:0000305};

Cofactor: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU01082, ECO:0000269|PubMed:19016841, ECO:0000269|PubMed:19700407, ECO:0000269|PubMed:21220116}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU01082, ECO:0000269|PubMed:19700407}; Note=Binds 2 manganese or magnesium ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU01082, ECO:0000269|PubMed:21220116};

Activity regulation: The phosphatase domain is activated by the anti- sigma factor kinase domain. {ECO:0000269|PubMed:19700407}.

Biophysicochemical properties: Kinetic parameters: KM=19.1 mM for pNPP {ECO:0000269|PubMed:19700407}; KM=31.2 mM for pNPP {ECO:0000269|PubMed:21220116}; Vmax=0.02 umol/min/mg enzyme with pNPP as substrate {ECO:0000269|PubMed:21220116}; Note=kcat is 14.2 min(-1) for pNPP hydrolysis. {ECO:0000269|PubMed:19700407}; pH dependence: Optimum pH is 8.5 for pNPP hydrolysis (PubMed:19016841). Optimum pH is 8.0 for pNPP hydrolysis (PubMed:19700407). {ECO:0000269|PubMed:19016841, ECO:0000269|PubMed:19700407}; Temperature dependence: Optimum temperature is 37 degrees Celsius for phosphatase activity. {ECO:0000269|PubMed:19016841};

Subunit: Exists in solution as both monomer and dimer (PubMed:21220116). Both the phosphorylated and unphosphorylated proteins form extended dimers (PubMed:19700407). Interacts with SigF (PubMed:30642988). Can efficiently bind to SigF independently of its autophosphorylation (PubMed:30642988). Interaction between SigF and Rv1364c is reduced significantly upon the phosphorylation of both proteins by PknD (PubMed:30642988). {ECO:0000269|PubMed:19700407, ECO:0000269|PubMed:21220116, ECO:0000269|PubMed:30642988}.

Induction: Induced by heat stress. {ECO:0000269|PubMed:17485404}.

Domain: Multidomain protein in which the components of the entire signal transduction cascade for SigF regulation appear to be encoded in a single polypeptide. Contains an N-terminal PAS sensor domain, followed by an adjacent PAC (PAS domain-associated C-terminus) region, a phosphatase domain, an anti-sigma factor kinase domain, and a C- terminal anti-anti-sigma factor domain (or substrate domain) (Probable). Phosphorylation at Ser-600 leads to a change in the overall shape of the dimer (PubMed:19700407). {ECO:0000269|PubMed:19700407, ECO:0000305|PubMed:19016841, ECO:0000305|PubMed:19700407}.

Ptm: Autophosphorylated (PubMed:30642988, PubMed:19700407). Phosphorylated by PknD on multiple threonine and serine residues (PubMed:30642988). Phosphorylation is antagonized by the phosphatase activity (PubMed:19700407). {ECO:0000269|PubMed:19700407, ECO:0000269|PubMed:30642988}.

Miscellaneous: Overexpression switch off espA induction under osmotic stress. {ECO:0000269|PubMed:30642988}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Taxonomy:		Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.



Function:		Primarily acts as an independent SigF regulator that is sensitive to the osmosensory signal, mediating the cross talk of PknD with the SigF regulon (PubMed:30642988). Possesses both phosphatase and kinase activities (PubMed:30642988, PubMed:19700407). The kinase domain functions as a classic anti-sigma factor-like kinase to phosphorylate the anti-anti-sigma factor domain at the canonical regulatory site, and the phosphatase domain antagonizes this activity (PubMed:19700407). {ECO:0000269\|PubMed:19700407, ECO:0000269\|PubMed:30642988}.


Catalytic activity:		Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000255\|PROSITE- ProRule:PRU01082, ECO:0000269\|PubMed:19700407, ECO:0000269\|PubMed:30642988};
Catalytic activity:		Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000255\|PROSITE- ProRule:PRU01082};
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:19700407, 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:0000305};
Cofactor:		Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255\|PROSITE-ProRule:PRU01082, ECO:0000269\|PubMed:19016841, ECO:0000269\|PubMed:19700407, ECO:0000269\|PubMed:21220116}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255\|PROSITE-ProRule:PRU01082, ECO:0000269\|PubMed:19700407}; Note=Binds 2 manganese or magnesium ions per subunit. {ECO:0000255\|PROSITE-ProRule:PRU01082, ECO:0000269\|PubMed:21220116};
Activity regulation:		The phosphatase domain is activated by the anti- sigma factor kinase domain. {ECO:0000269\|PubMed:19700407}.
Biophysicochemical properties:		Kinetic parameters: KM=19.1 mM for pNPP {ECO:0000269\|PubMed:19700407}; KM=31.2 mM for pNPP {ECO:0000269\|PubMed:21220116}; Vmax=0.02 umol/min/mg enzyme with pNPP as substrate {ECO:0000269\|PubMed:21220116}; Note=kcat is 14.2 min(-1) for pNPP hydrolysis. {ECO:0000269\|PubMed:19700407}; pH dependence: Optimum pH is 8.5 for pNPP hydrolysis (PubMed:19016841). Optimum pH is 8.0 for pNPP hydrolysis (PubMed:19700407). {ECO:0000269\|PubMed:19016841, ECO:0000269\|PubMed:19700407}; Temperature dependence: Optimum temperature is 37 degrees Celsius for phosphatase activity. {ECO:0000269\|PubMed:19016841};
Subunit:		Exists in solution as both monomer and dimer (PubMed:21220116). Both the phosphorylated and unphosphorylated proteins form extended dimers (PubMed:19700407). Interacts with SigF (PubMed:30642988). Can efficiently bind to SigF independently of its autophosphorylation (PubMed:30642988). Interaction between SigF and Rv1364c is reduced significantly upon the phosphorylation of both proteins by PknD (PubMed:30642988). {ECO:0000269\|PubMed:19700407, ECO:0000269\|PubMed:21220116, ECO:0000269\|PubMed:30642988}.
Induction:		Induced by heat stress. {ECO:0000269\|PubMed:17485404}.
Domain:		Multidomain protein in which the components of the entire signal transduction cascade for SigF regulation appear to be encoded in a single polypeptide. Contains an N-terminal PAS sensor domain, followed by an adjacent PAC (PAS domain-associated C-terminus) region, a phosphatase domain, an anti-sigma factor kinase domain, and a C- terminal anti-anti-sigma factor domain (or substrate domain) (Probable). Phosphorylation at Ser-600 leads to a change in the overall shape of the dimer (PubMed:19700407). {ECO:0000269\|PubMed:19700407, ECO:0000305\|PubMed:19016841, ECO:0000305\|PubMed:19700407}.
Ptm:		Autophosphorylated (PubMed:30642988, PubMed:19700407). Phosphorylated by PknD on multiple threonine and serine residues (PubMed:30642988). Phosphorylation is antagonized by the phosphatase activity (PubMed:19700407). {ECO:0000269\|PubMed:19700407, ECO:0000269\|PubMed:30642988}.
Miscellaneous:		Overexpression switch off espA induction under osmotic stress. {ECO:0000269\|PubMed:30642988}.