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(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
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Identifier, protein and gene names
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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
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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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Cytoplasm | |
ATP-binding | |
Chaperone | |
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella> | |
Stress response | |
end case | |
Nucleotide-binding |
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 |
Cross-references
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Pfam | PF00004; AAA; 1; |
Pfam | PF07724; AAA_2; 1; |
Pfam | PF10431; ClpB_D2-small; 1; |
NCBIfam | TIGR00390; HslU; 1; |
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 |
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. |