HAMAP annotation rule: MF_00249
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Accession MF_00249
Dates 1-JUN-2001 (Created)
9-JUN-2011 (Last updated, Version 27)
Data class Protein
Names HslU



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 hslU
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 (By similarity).
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 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).

case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
INDUCTION: By heat shock (By similarity).
end case

SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
Pfam PF00004; AAA; 1;
PF07724; AAA_2; 1;
PF10431; ClpB_D2-small; 1;
TIGRFAMs TIGR00390; HslU; 1;

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

GO:0005524; Molecular function: ATP binding.
GO:0016887; Molecular function: ATPase activity.
GO:0043335; Biological process: protein unfolding.
GO:0005737; Cellular component: cytoplasm.
GO:0009376; Cellular component: HslUV protease complex.
From: HSLU_ECOLI (P0A6H5)
Key     From     To       Description   Condition   FTGroup
NP_BIND     60     65       ATP (By similarity)   G-[VIC]-G-K-T-E  
BINDING     18     18       ATP; via amide nitrogen and carbonyl oxygen (By similarity)   [IV]  
BINDING     256     256       ATP (By similarity)   D  
BINDING     321     321       ATP (By similarity)   E  
BINDING     393     393       ATP (By similarity)   R  



Size range: 430-491 amino acids
Related UniRules: MF_00175 (CLPX)
Template: P0A6H5 (HSLU_ECOLI); P43773 (HSLU_HAEIN); P39778 (CLPY_BACSU); Q9WYZ2 (HSLU_THEMA): [Recover all]
Scope: Bacteria
Fusion: Nter: None; Cter: None
Duplicate: None
Plasmid encoded: 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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