IED ID | IndEnz0002014764 |
Enzyme Type ID | protease014764 |
Protein Name |
ATP-dependent protease ATPase subunit HslU Unfoldase HslU |
Gene Name | hslU SE_0930 |
Organism | Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus epidermidis Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) |
Enzyme Sequence | MDTNGIKLTPKDIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLKEEEKQEIAPKNILMIGPTGVGKTEIARRMAKIVGAPFIKVEATKFTEVGYVGRDVESMVRDLVDVAVRLVKDEKKSLVKDEATKKANDKLVKLLVPSLKKKAAQGNNPLENLFGGAIPNFGQNQDEEEEPPTEEIKTKRSEIKKQLEQGKLENEKVRIKVEQDPASMGMLGTNQNQQIQDMMNQLMPKKKVEREVSVETARKILADDFADELIDQETANQQALELAEQMGIIFIDEIDKVATNNQNSGQDVSRQGVQRDILPILEGSMIQTKYGTVNTEHMLFIGAGAFHVSKPSDLIPELQGRFPIRVELESLSVEDFVRILTEPKLSLVKQYEALLQTEEVTVNFSEDAIQRLAEIAYQVNQDTDNIGARRLHTILEKMLEDLSFEAPSMPNAVVDITPQYVDDKLKSISTNKDLSAFIL |
Enzyme Length | 467 |
Uniprot Accession Number | Q8CPH0 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 22; /note=ATP; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 280; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 345; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 417; /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 64..69; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249 |
Features | Binding site (4); Chain (1); Nucleotide binding (1); Region (1) |
Keywords | ATP-binding;Chaperone;Cytoplasm;Nucleotide-binding |
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 | 52,454 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |