Detail Information for IndEnz0002015911
IED ID IndEnz0002015911
Enzyme Type ID protease015911
Protein Name ATP-dependent protease ATPase subunit HslU
Unfoldase HslU
Gene Name hslU Bphy_0069
Organism Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815) (Burkholderia phymatum)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Paraburkholderia Paraburkholderia phymatum Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815) (Burkholderia phymatum)
Enzyme Sequence MSTMTPAEIVSELDKHIIGQNRAKKAVAVALRNRWRRQQVDEPLRQEITPKNILMIGPTGVGKTEIARRLAKLADAPFIKIEATKFTEVGYVGRDVDSIVRDLIEISVKQTRETEMRKMRTKAEDLAEDRILDILLPGARTVGFGSGTSEASGDESNTTRQTFRKRLREGALDDKEIELDIEMQAPAMDIMGPPGMEDMTEQIRSMFANLGGGKKTRRKVKVKEALKLLTDEEASKMLNDEEVKTKAVQNVEQNGIVFLDEIDKIASRSEAGGGEVSRQGVQRDLLPLVEGTTINTKYGMVKTDHILFIASGAFHLAKPSDLIPELQGRFPIRVELDSLSVKDFESILVATDASLVKQYQALLATEDVHLEFADDGIRRLAEIAFSVNEKTENIGARRLYTVIEKLLEEVSFSAGNHTGKSVLIDAAYVDRALNDVAQDEDLSRYVL
Enzyme Length 447
Uniprot Accession Number B2JJX7
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 260; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 325; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 397; /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 49,682
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda