| IED ID | IndEnz0002006830 |
| Enzyme Type ID | protease006830 |
| Protein Name |
ATP-dependent protease ATPase subunit HslU Unfoldase HslU |
| Gene Name | hslU HI_0497 |
| Organism | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pasteurellales Pasteurellaceae Haemophilus Haemophilus influenzae Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
| Enzyme Sequence | MSEMTPREIVSELDQHIIGQADAKRAVAIALRNRWRRMQLQEPLRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDSAMKLVRQQEIAKNRARAEDVAEERILDALLPPAKNQWGEVENHDSHSSTRQAFRKKLREGQLDDKEIEIDVSAGVSMGVEIMAPPGMEEMTNQLQSLFQNLGSDKTKKRKMKIKDALKALIDDEAAKLINPEELKQKAIDAVEQNGIVFIDEIDKICKKGEYSGADVSREGVQRDLLPLVEGSTVSTKHGMVKTDHILFIASGAFQVARPSDLIPELQGRLPIRVELTALSAADFERILTEPHASLTEQYKALMATEGVNIAFTTDAVKKIAEAAFRVNEKTENIGARRLHTVMERLMDKISFSASDMNGQTVNIDAAYVADALGEVVENEDLSRFIL |
| Enzyme Length | 444 |
| Uniprot Accession Number | P43773 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 18; /note=ATP; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000269|PubMed:11106733; BINDING 257; /note=ATP; /evidence=ECO:0000250; BINDING 322; /note=ATP; /evidence=ECO:0000250; BINDING 394; /note=ATP; /evidence=ECO:0000250 |
| 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 60..65; /note=ATP; /evidence=ECO:0000269|PubMed:11106733; NP_BIND 306..309; /note=ATP; /evidence=ECO:0000269|PubMed:11106733 |
| Features | Beta strand (14); Binding site (4); Chain (1); Compositional bias (1); Helix (21); Nucleotide binding (2); Region (1); Turn (3) |
| Keywords | 3D-structure;ATP-binding;Chaperone;Cytoplasm;Nucleotide-binding;Reference proteome |
| Interact With | P43772 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1G3I; 1G41; 1IM2; 1KYI; 1OFH; 1OFI; |
| Mapped Pubmed ID | 11709174; 12054822; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,372 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |