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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
Scope(s) Bacteria
Template(s) P0A6H5 (HSLU_ECOLI); P43773 (HSLU_HAEIN); P39778 (CLPY_BACSU); Q9WYZ2 (HSLU_THEMA); [ Recover all ]
Triggered by HAMAP; MF_00249 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier HSLU
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 Name=hslU;

Comments [?]

FUNCTIONATPase 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.
SUBUNITA 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.
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
INDUCTIONBy heat shock.
end case
SIMILARITYBelongs to the ClpX chaperone family. HslU subfamily.

Keywords [?]

case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
Stress response
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;
Pfam PF07724; AAA_2; 1;
Pfam PF10431; ClpB_D2-small; 1;
NCBIfam TIGR00390; HslU; 1;

Features [?]

Key From To Description Tag Condition FTGroup
BINDING 60 65 /ligand="ATP"
BINDING 18 18 /ligand="ATP"
BINDING 256 256 /ligand="ATP"
BINDING 321 321 /ligand="ATP"
BINDING 393 393 /ligand="ATP"

Additional information [?]

Size range 430-491 amino acids
Related rules MF_00175
Fusion Nter: None Cter: 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.

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