Detail Information for IndEnz0002003417
IED ID IndEnz0002003417
Enzyme Type ID protease003417
Protein Name ATP-dependent protease ATPase subunit HslU
Unfoldase HslU
Gene Name hslU FTN_0996
Organism Francisella tularensis subsp. novicida (strain U112)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Thiotrichales Francisellaceae Francisella Francisella tularensis Francisella novicida Francisella tularensis subsp. novicida (strain U112)
Enzyme Sequence MTQIMTPKTIVHELERHIIGQNDAKKAVAIALRNRWRRMQLDNEMRQEVTPKNILMIGPTGVGKTEIARRLAKLADAPFIKVEATKFTEVGYVGKDVESIIRDLVETAVKMKREEAKEKVTEKAARLAEDRILDVLIPPARTSESKVGFANEPAEDAASKKEKENKTREIFRKKIQKGELDDKEIEIEVAVAPKTIGVMGPPGMEDMTSQLQDLFSSLSTDKKKNKKMRIKDAIKLAQDEEAAKLVNEEDIKARALEAVEQNGIVFLDEIDKVCRKSSNSGADVSREGVQRDLLPLVEGSTVSTKYGMIKTDHILFIASGAFHVAKPSDLIPELQGRLPIRVELKSLEIEDFVRILREPDCSILKQYIALMKTEGVDLSFEEDAIRKIAEIAYKVNEEVENIGARRLHTVMERLLEEISFDAPELVEKNINITTDYVNEKLGNLVKNKDLSQYIL
Enzyme Length 455
Uniprot Accession Number A0Q6L9
Absorption
Active Site
Activity Regulation
Binding Site BINDING 19; /note=ATP; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 268; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 333; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 405; /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 61..66; /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 51,270
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda