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UniProt functional annotation for P0A6H6 | ||
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| UniProt codes: P0A6H6, P32168. |
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| Organism: | |
Escherichia coli O157:H7. |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| 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}. |
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| 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:0000255|HAMAP- Rule:MF_00249}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00249}. |
| Induction: | |
By heat shock. {ECO:0000255|HAMAP-Rule:MF_00249}. |
| Similarity: | |
Belongs to the ClpX chaperone family. HslU subfamily. {ECO:0000255|HAMAP-Rule:MF_00249}. |
Annotations taken from UniProtKB at the EBI.