serine kinase [Ancylobacter sp. TS-1]
Protein Classification
phosphoenolpyruvate carboxykinase (ATP)( domain architecture ID 366276)
phosphoenolpyruvate carboxykinase (ATP) catalyzes the phosphorylation and decarboxylation of oxaloacetate to form phosphoenolpyruvate using ATP
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| HprK super family | cl30706 | Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction ... |
161-193 | 1.40e-04 | ||
Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction mechanisms]; The actual alignment was detected with superfamily member COG1493: Pssm-ID: 441102 [Multi-domain] Cd Length: 142 Bit Score: 41.32 E-value: 1.40e-04
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| Name | Accession | Description | Interval | E-value | ||
| HprK | COG1493 | Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction ... |
161-193 | 1.40e-04 | ||
Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction mechanisms]; Pssm-ID: 441102 [Multi-domain] Cd Length: 142 Bit Score: 41.32 E-value: 1.40e-04
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| HprK_C | cd01918 | HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the ... |
161-193 | 3.03e-04 | ||
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: 40.68 E-value: 3.03e-04
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| PRK04195 | PRK04195 | replication factor C large subunit; Provisional |
161-180 | 3.28e-03 | ||
replication factor C large subunit; Provisional Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 39.13 E-value: 3.28e-03
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| Hpr_kinase_C | pfam07475 | HPr Serine kinase C-terminal domain; This family represents the C terminal kinase domain of ... |
161-193 | 3.85e-03 | ||
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: 37.46 E-value: 3.85e-03
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| Name | Accession | Description | Interval | E-value | ||
| HprK | COG1493 | Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction ... |
161-193 | 1.40e-04 | ||
Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction mechanisms]; Pssm-ID: 441102 [Multi-domain] Cd Length: 142 Bit Score: 41.32 E-value: 1.40e-04
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| HprK_C | cd01918 | HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the ... |
161-193 | 3.03e-04 | ||
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: 40.68 E-value: 3.03e-04
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| COG1223 | COG1223 | Predicted ATPase, AAA+ superfamily [General function prediction only]; |
151-181 | 1.81e-03 | ||
Predicted ATPase, AAA+ superfamily [General function prediction only]; Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 39.48 E-value: 1.81e-03
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| PRK04195 | PRK04195 | replication factor C large subunit; Provisional |
161-180 | 3.28e-03 | ||
replication factor C large subunit; Provisional Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 39.13 E-value: 3.28e-03
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| Hpr_kinase_C | pfam07475 | HPr Serine kinase C-terminal domain; This family represents the C terminal kinase domain of ... |
161-193 | 3.85e-03 | ||
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: 37.46 E-value: 3.85e-03
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| RecA-like_ClpB_Hsp104-like | cd19499 | Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
139-184 | 5.10e-03 | ||
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion. Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 37.54 E-value: 5.10e-03
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