HAMAP rule MF_00249
General rule information
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Accession | MF_00249 |
Dates | 1-JUN-2001 (Created) 1-JUN-2023 (Last updated, Version 34) |
Name | HslU |
Scope | Bacteria |
Templates | P0A6H5 (HSLU_ECOLI); P43773 (HSLU_HAEIN); P39778 (CLPY_BACSU); Q9WYZ2 (HSLU_THEMA): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
Protein name |
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end case
case not <OC:Escherichia> and not <OC:Shigella> and not <OC:Salmonella>
Protein name |
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end case
Gene name |
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Comments
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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. |
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. |
Subcellular location | Cytoplasm. |
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
Induction | By heat shock. |
end case
Similarity | Belongs to the ClpX chaperone family. HslU subfamily. |
Keywords
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case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
end case
Gene Ontology
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GO:0005524; Molecular function: ATP binding.
GO:0036402; Molecular function: proteasome-activating activity.
GO:0043335; Biological process: protein unfolding.
GO:0005737; Cellular component: cytoplasm.
GO:0009376; Cellular component: HslUV protease complex.
GO:0036402; Molecular function: proteasome-activating activity.
GO:0043335; Biological process: protein unfolding.
GO:0005737; Cellular component: cytoplasm.
GO:0009376; Cellular component: HslUV protease complex.
Cross-references
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Features
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From: HSLU_ECOLI (P0A6H5) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 60 | 65 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | G-[VIC]-G-K-T-E | ||||||||
BINDING | 18 | 18 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | [IV] | ||||||||
BINDING | 256 | 256 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | D | ||||||||
BINDING | 321 | 321 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | E | ||||||||
BINDING | 393 | 393 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | R |
Additional information
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Size range | 430-491 amino acids |
Related rules | MF_00175 (CLPX) |
Fusion | None |
Comments | The protease subunit of the HslUV complex is described in MF_00248. Unlike in E.coli, H.influenzae and T.maritima, the family member in B.subtilis (ClpY) was shown to be part of a complex (ClpQY) with serine protease activity and not threonine protease activity. |