Detail Information for IndEnz0002003126
IED ID IndEnz0002003126
Enzyme Type ID protease003126
Protein Name ATP-dependent protease ATPase subunit HslU
Unfoldase HslU
Gene Name hslU VSAL_I2739
Organism Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238))
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Aliivibrio Aliivibrio salmonicida Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238))
Enzyme Sequence MSEMTPREIVHELDSHIIGQDKAKRSVAIALRNRWRRMQLQPELRAEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDVAIKMTHQQAVEKVKFRAEEQAEDRILDILLPPARDAWGKNEEGDNDSGTRQSFRKKLREGKLDDKEIDVDVAAPQVGVEIMAPPGMEEMTNQLQGMFQNLSGGETTKKRKMKIKDALKALAEEEGAKLVNPEELKEQAIFNVENHGIVFIDEIDKICKGSNSQSGDVSREGVQRDLLPLVEGSTVSTKHGMVRTDHMLFITSGAFQMAKPSDLIPELQGRLPIRVELEALTANDFKRILTEPNASLTEQYIALLATENVNIEFTEDGISRIAESAFRVNETTENIGARRLHTVMERLMEEISYDASEKGGDSLTVDDAYVTSRLGELIENEDLSRFIL
Enzyme Length 444
Uniprot Accession Number B6EML9
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 257; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 322; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 394; /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;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 49,650
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda