| IED ID | IndEnz0002016177 |
| Enzyme Type ID | protease016177 |
| Protein Name |
ATP-dependent protease ATPase subunit HslU Unfoldase HslU |
| Gene Name | hslU HPP12_0522 |
| Organism | Helicobacter pylori (strain P12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Epsilonproteobacteria Campylobacterales Helicobacteraceae Helicobacter Helicobacter pylori (Campylobacter pylori) Helicobacter pylori (strain P12) |
| Enzyme Sequence | MSKLNMTPREIVAYLDEYIIGQKEAKKSIAIAFRNRYRRLQLEKSLQEEITPKNILMIGSTGVGKTEIARRIAKIMELPFVKVEASKYTEVGFVGRDVESMVRDLVNNSVLLVENEHKEKLKDKIEEAVIEKIAKKLLPPLPSGVSEEKKQEYANSLLKMQQRIAQGELDSREIEIEVRKKSIEIDSNVPPEILRVQENLIKVFHKEQDKVKKTLSVKEAKEALKAEISDTLLDSEAIKMEGLKRAESSGVIFIDEIDKIAVSSKEGSRQDPSKEGVQRDLLPIVEGSVVNTKYGSIKTEHILFIAAGAFHLSKPSDLIPELQGRFPLRVELENLTEEIMYMILTQTKTSIIKQYQALLKVEGVGIAFEDDAIKELAKLSYNANQKSEDIGARRLHTTIEKVLEDISFEAEDYSGQKVTITKELVQSKLEDLVADENLVKYIL |
| Enzyme Length | 443 |
| Uniprot Accession Number | B6JL98 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 20; /note=ATP; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 255; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 321; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 393; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. {ECO:0000255|HAMAP-Rule:MF_00249}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 62..67; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249 |
| Features | Binding site (4); Chain (1); Nucleotide binding (1) |
| Keywords | ATP-binding;Chaperone;Cytoplasm;Nucleotide-binding;Stress response |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00249}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,106 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |