IED ID | IndEnz0002014835 |
Enzyme Type ID | protease014835 |
Protein Name |
ATP-dependent protease ATPase subunit HslU Unfoldase HslU |
Gene Name | hslU Xaut_2296 |
Organism | Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Hyphomicrobiales Xanthobacteraceae Xanthobacter Xanthobacter autotrophicus Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) |
Enzyme Sequence | MSDFSPREIVSELDRHIVGQANAKRAVAIALRNRWRRQQLDDKLREEVLPKNILMIGPTGVGKTEISRRLARLAGAPFLKVEATKFTEVGYVGRDVEQIVRDLVEVGIGLVREARRKDVQAKAHLAAENRVLDALVGATASPATRDAFRKRLRAGELDDKEVEIEVQAGGQGMPMFEIPGMPGTQMGAVNLGDMLGKAFGGRSKPRRVNVKEAHPLLLAEEADKLIDQDAIVQDAIHQVENNGIVFLDEIDKIAGREGRSGADVSREGVQRDLLPLIEGTTVSTKHGPVKTDHILFIASGAFHVSKPSDLLPELQGRLPIRVELEALTRADFVRILTETEASLVKQSVALMGTEGVTLTITTDAVEAIADAAVEVNSNVENIGARRLQTVIERVLDDLSFSAPDRSGETVVVDAEYVRSRVADLARNADLSRFIL |
Enzyme Length | 435 |
Uniprot Accession Number | A7IHP6 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 18; /note=ATP; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 248; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 313; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 385; /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 60..65; /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;Reference proteome;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 | 47,464 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |