UniProt functional annotation for P0A6H5



	UniProt functional annotation for P0A6H5

UniProt codes: P0A6H5, P32168.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

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:0000269|PubMed:10419524, ECO:0000269|PubMed:10452560, ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8650174, ECO:0000269|PubMed:8662828, ECO:0000269|PubMed:9288941, ECO:0000269|PubMed:9393683}.

Biophysicochemical properties: Kinetic parameters: KM=0.31 mM for ATP (in the absence of HslV) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; KM=0.28 mM for ATP (in the presence of HslV) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; KM=5.2 uM for Arc-MYL-st11 (at 37 degrees Celsius) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; Vmax=57 pmol/min/mg enzyme (in the absence of HslV) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; Vmax=213 pmol/min/mg enzyme (in the presence of HslV) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; Note=Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.; Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828};

Subunit: A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP. {ECO:0000269|PubMed:11709174, ECO:0000269|PubMed:15983416}.

Subcellular location: Cytoplasm.

Induction: By heat shock. {ECO:0000269|PubMed:8244018}.

Similarity: Belongs to the ClpX chaperone family. HslU subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



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:0000269\|PubMed:10419524, ECO:0000269\|PubMed:10452560, ECO:0000269\|PubMed:15696175, ECO:0000269\|PubMed:8650174, ECO:0000269\|PubMed:8662828, ECO:0000269\|PubMed:9288941, ECO:0000269\|PubMed:9393683}.


Biophysicochemical properties:		Kinetic parameters: KM=0.31 mM for ATP (in the absence of HslV) {ECO:0000269\|PubMed:15696175, ECO:0000269\|PubMed:8662828}; KM=0.28 mM for ATP (in the presence of HslV) {ECO:0000269\|PubMed:15696175, ECO:0000269\|PubMed:8662828}; KM=5.2 uM for Arc-MYL-st11 (at 37 degrees Celsius) {ECO:0000269\|PubMed:15696175, ECO:0000269\|PubMed:8662828}; Vmax=57 pmol/min/mg enzyme (in the absence of HslV) {ECO:0000269\|PubMed:15696175, ECO:0000269\|PubMed:8662828}; Vmax=213 pmol/min/mg enzyme (in the presence of HslV) {ECO:0000269\|PubMed:15696175, ECO:0000269\|PubMed:8662828}; Note=Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.; Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269\|PubMed:15696175, ECO:0000269\|PubMed:8662828};
Subunit:		A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP. {ECO:0000269\|PubMed:11709174, ECO:0000269\|PubMed:15983416}.
Subcellular location:		Cytoplasm.
Induction:		By heat shock. {ECO:0000269\|PubMed:8244018}.
Similarity:		Belongs to the ClpX chaperone family. HslU subfamily. {ECO:0000305}.