Detail Information for IndEnz0002014807
IED ID IndEnz0002014807
Enzyme Type ID protease014807
Protein Name ATP-dependent protease ATPase subunit HslU
Unfoldase HslU
Gene Name hslU VC0395_A2247 VC395_2787
Organism Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio cholerae Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Enzyme Sequence MSEMTPREIVSELNRHIIGQDKAKRAVAIALRNRWRRMQLEESLRVEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVESIIRDLTDVAVKLTHQQAMEKVKFRAEELAEERVLDALLPPPRDAWGQAEQKEENSSTRQVFRKKLREGQLNDKEIEINVAVPQMGVEIMAPPGMEEMTNQLQGLFQNLAGDTKKKRKMKIKDALKALVEEEAAKLVNQEELKEQAIYNVENNGIVFIDEIDKICKRGEVSGPDVSREGVQRDLLPLIEGSTVSTKHGMVRTDHILFIASGAFQVAKPSDLIPELQGRLPIRVELEALSSNDFKRILTEPKASLTEQYVALMKTEQVDVQFTEDGIKQIADAAWQVNETTENIGARRLHTVLERLMDEISFDATEKAGQAFVIDAAYVKARLGELVEDEDLSRFIL
Enzyme Length 443
Uniprot Accession Number A5F4X3
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 256; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 321; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00249; BINDING 393; /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
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 49,872
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda