| IED ID | IndEnz0002006410 |
| Enzyme Type ID | protease006410 |
| Protein Name |
GTPase HflX GTP-binding protein HflX |
| Gene Name | hflX b4173 JW4131 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MFDRYDAGEQAVLVHIYFTQDKDMEDLQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLFDHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQLETDRRLLRNRIVQIQSRLERVEKQREQGRQSRIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIEAVNTVLEEIDAHEIPTLLVMNKIDMLEDFEPRIDRDEENKPNRVWLSAQTGAGIPQLFQALTERLSGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEWMEEDGSVSLQVRMPIVDWRRLCKQEPALIDYLI |
| Enzyme Length | 426 |
| Uniprot Accession Number | P25519 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Intrinsic GTPase activity is very slow and can be stimulated by the presence of 50S ribosomal subunits or 70S ribosomes. GTPase activity is inhibited by ATP. {ECO:0000269|PubMed:19109926, ECO:0000269|PubMed:19181811, ECO:0000269|PubMed:19824612}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis. In vitro, also exhibits ATPase activity. {ECO:0000255|HAMAP-Rule:MF_00900, ECO:0000269|PubMed:19109926, ECO:0000269|PubMed:19181811, ECO:0000269|PubMed:19824612}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 204..211; /note=GTP; /evidence=ECO:0000255|HAMAP-Rule:MF_00900; NP_BIND 229..233; /note=GTP; /evidence=ECO:0000255|HAMAP-Rule:MF_00900; NP_BIND 251..254; /note=GTP; /evidence=ECO:0000255|HAMAP-Rule:MF_00900; NP_BIND 317..320; /note=GTP; /evidence=ECO:0000255|HAMAP-Rule:MF_00900; NP_BIND 343..345; /note=GTP; /evidence=ECO:0000255|HAMAP-Rule:MF_00900 |
| Features | Chain (1); Domain (1); Frameshift (1); Metal binding (2); Nucleotide binding (5); Sequence conflict (2) |
| Keywords | 3D-structure;ATP-binding;Cytoplasm;GTP-binding;Magnesium;Metal-binding;Nucleotide-binding;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900, ECO:0000269|PubMed:19181811}. Note=May associate with membranes. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (2) |
| Cross Reference PDB | 5ADY; 5ZZM; |
| Mapped Pubmed ID | 24561554; 26458047; 29930203; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,327 |
| Kinetics | |
| Metal Binding | METAL 211; /note=Magnesium; /evidence=ECO:0000255|HAMAP-Rule:MF_00900; METAL 231; /note=Magnesium; /evidence=ECO:0000255|HAMAP-Rule:MF_00900 |
| Rhea ID | |
| Cross Reference Brenda |