| IED ID | IndEnz0002015593 |
| Enzyme Type ID | protease015593 |
| Protein Name |
ATP-dependent protease ATPase subunit HslU Heat shock protein HslU Unfoldase HslU |
| Gene Name | hslU htpI b3931 JW3902 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDAAVKMVRVQAIEKNRYRAEELAEERILDVLIPPAKNNWGQTEQQQEPSAARQAFRKKLREGQLDDKEIEIDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQIAKPSDLIPELQGRLPIRVELQALTTSDFERILTEPNASITVQYKALMATEGVNIEFTDSGIKRIAEAAWQVNESTENIGARRLHTVLERLMEEISYDASDLSGQNITIDADYVSKHLDALVADEDLSRFIL |
| Enzyme Length | 443 |
| Uniprot Accession Number | P0A6H5 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 18; /note=ATP; via amide nitrogen and carbonyl oxygen; BINDING 256; /note=ATP; BINDING 321; /note=ATP; BINDING 393; /note=ATP |
| 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:0000269|PubMed:10419524, ECO:0000269|PubMed:10452560, ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8650174, ECO:0000269|PubMed:8662828, ECO:0000269|PubMed:9288941, ECO:0000269|PubMed:9393683}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 60..65; /note=ATP |
| Features | Beta strand (13); Binding site (4); Chain (1); Helix (25); Mutagenesis (18); Nucleotide binding (1); Turn (4) |
| Keywords | 3D-structure;ATP-binding;Chaperone;Cytoplasm;Nucleotide-binding;Reference proteome;Stress response |
| Interact With | Itself; P0A7B8; P0AFZ5 |
| Induction | INDUCTION: By heat shock. {ECO:0000269|PubMed:8244018}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (14) |
| Cross Reference PDB | 1DO0; 1DO2; 1E94; 1G4A; 1G4B; 1HQY; 1HT1; 1HT2; 1YYF; 5JI3; 5TXV; 6PXI; 6PXK; 6PXL; |
| Mapped Pubmed ID | 11250202; 12670962; 15004283; 15690043; 16606699; 16858726; 19395483; 21803990; 27667691; 28223361; 33472065; 9177170; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,594 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.31 mM for ATP (in the absence of HslV) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; KM=0.28 mM for ATP (in the presence of HslV) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; KM=5.2 uM for Arc-MYL-st11 (at 37 degrees Celsius) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; Vmax=57 pmol/min/mg enzyme (in the absence of HslV) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; Vmax=213 pmol/min/mg enzyme (in the presence of HslV) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; Note=Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.25.2; |