HPr kinase/phosphorylase catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of 'Ser-46' in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS); also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr)
Hpr(Ser) kinase/phosphatase; Members of this family are the bifunctional enzyme, HPr kinase ...
3-303
7.51e-139
Hpr(Ser) kinase/phosphatase; Members of this family are the bifunctional enzyme, HPr kinase/phosphatase. All members of the seed alignment (n=57) have a gene tightly clustered with a gene for the phospocarrier protein HPr, its target. [Regulatory functions, Protein interactions, Signal transduction, PTS]
Pssm-ID: 273214 Cd Length: 300 Bit Score: 394.53 E-value: 7.51e-139
HPr Serine kinase C-terminal domain; This family represents the C terminal kinase domain of ...
129-299
3.62e-96
HPr Serine kinase C-terminal domain; This family represents the C terminal kinase domain of Hpr Serine/threonine kinase PtsK. This kinase is the sensor in a multicomponent phosphorelay system in control of carbon catabolic repression in bacteria. This kinase in unusual in that it recognizes the tertiary structure of its target and is a member of a novel family unrelated to any previously described protein phosphorylating enzymes. X-ray analysis of the full-length crystalline enzyme from Staphylococcus xylosus at a resolution of 1.95 A shows the enzyme to consist of two clearly separated domains that are assembled in a hexameric structure resembling a three-bladed propeller.
Pssm-ID: 462176 Cd Length: 171 Bit Score: 281.29 E-value: 3.62e-96
HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the ...
133-282
5.23e-62
HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of Ser-46 of HPr and its dephosphorylation by phosphorolysis. The latter reaction uses inorganic phosphate as substrate and produces pyrophosphate. Phosphoenolpyruvate carboxykinase (PEPCK) and the C-terminal catalytic domain of HprK/P are structurally similar with conserved active site residues suggesting these two phosphotransferases have related functions. The HprK/P N-terminal domain is structurally similar to the N-terminal domains of the MurE and MurF amino acid ligases.
Pssm-ID: 238899 Cd Length: 149 Bit Score: 193.61 E-value: 5.23e-62
Hpr(Ser) kinase/phosphatase; Members of this family are the bifunctional enzyme, HPr kinase ...
3-303
7.51e-139
Hpr(Ser) kinase/phosphatase; Members of this family are the bifunctional enzyme, HPr kinase/phosphatase. All members of the seed alignment (n=57) have a gene tightly clustered with a gene for the phospocarrier protein HPr, its target. [Regulatory functions, Protein interactions, Signal transduction, PTS]
Pssm-ID: 273214 Cd Length: 300 Bit Score: 394.53 E-value: 7.51e-139
HPr Serine kinase C-terminal domain; This family represents the C terminal kinase domain of ...
129-299
3.62e-96
HPr Serine kinase C-terminal domain; This family represents the C terminal kinase domain of Hpr Serine/threonine kinase PtsK. This kinase is the sensor in a multicomponent phosphorelay system in control of carbon catabolic repression in bacteria. This kinase in unusual in that it recognizes the tertiary structure of its target and is a member of a novel family unrelated to any previously described protein phosphorylating enzymes. X-ray analysis of the full-length crystalline enzyme from Staphylococcus xylosus at a resolution of 1.95 A shows the enzyme to consist of two clearly separated domains that are assembled in a hexameric structure resembling a three-bladed propeller.
Pssm-ID: 462176 Cd Length: 171 Bit Score: 281.29 E-value: 3.62e-96
HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the ...
133-282
5.23e-62
HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of Ser-46 of HPr and its dephosphorylation by phosphorolysis. The latter reaction uses inorganic phosphate as substrate and produces pyrophosphate. Phosphoenolpyruvate carboxykinase (PEPCK) and the C-terminal catalytic domain of HprK/P are structurally similar with conserved active site residues suggesting these two phosphotransferases have related functions. The HprK/P N-terminal domain is structurally similar to the N-terminal domains of the MurE and MurF amino acid ligases.
Pssm-ID: 238899 Cd Length: 149 Bit Score: 193.61 E-value: 5.23e-62
HPr Serine kinase N terminus; This family represents the N-terminal region of Hpr Serine ...
3-127
3.88e-50
HPr Serine kinase N terminus; This family represents the N-terminal region of Hpr Serine/threonine kinase PtsK. This kinase is the sensor in a multicomponent phospho-relay system in control of carbon catabolic repression in bacteria. This kinase in unusual in that it recognizes the tertiary structure of its target and is a member of a novel family unrelated to any previously described protein phosphorylating enzymes. X-ray analysis of the full-length crystalline enzyme from Staphylococcus xylosus at a resolution of 1.95 A shows the enzyme to consist of two clearly separated domains that are assembled in a hexameric structure resembling a three-bladed propeller. The blades are formed by two N-terminal domains each, and the compact central hub assembles the C-terminal kinase domains.
Pssm-ID: 460614 Cd Length: 125 Bit Score: 162.18 E-value: 3.88e-50
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ...
135-179
7.37e-09
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (ATP or GTP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity (the ATP-, and GTP-dependent groups).HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of HPr and its dephosphorylation by phosphorolysis. PEPCK and the C-terminal catalytic domain of HprK/P are structurally similar with conserved active site residues suggesting that these two phosphotransferases have related functions.
Pssm-ID: 238418 [Multi-domain] Cd Length: 107 Bit Score: 52.68 E-value: 7.37e-09
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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