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HAMAP rule MF_00249

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General rule information [?]

Accession MF_00249
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 34)
Name HslU
Templates P0A6H5 (HSLU_ECOLI); P43773 (HSLU_HAEIN); P39778 (CLPY_BACSU); Q9WYZ2 (HSLU_THEMA): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
Protein name
RecName: Full=ATP-dependent protease ATPase subunit HslU;
AltName: Full=Heat shock protein HslU;
AltName: Full=Unfoldase HslU;
end case
case not <OC:Escherichia> and not <OC:Shigella> and not <OC:Salmonella>
Protein name
RecName: Full=ATP-dependent protease ATPase subunit HslU;
AltName: Full=Unfoldase HslU;
end case
Gene name

Comments [?]

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 [?]

case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
end case

Gene Ontology [?]

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.

Cross-references [?]

Pfam PF00004; AAA; 1;
PF07724; AAA_2; 1;
PF10431; ClpB_D2-small; 1;
NCBIfam TIGR00390; HslU; 1;

Features [?]

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 [?]

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.