AC   MF_00249;
DC   Protein; auto
TR   HAMAP; MF_00249; -; 1; level=0
XX
Names: HslU
XX
ID   HSLU
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU;
DE   AltName: Full=Heat shock protein HslU;
DE   AltName: Full=Unfoldase HslU;
end case
case not <OC:Escherichia> and not <OC:Shigella> and not <OC:Salmonella>
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU;
DE   AltName: Full=Unfoldase HslU;
end case
GN   Name=hslU;
XX
CC   -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex; this
CC       subunit has chaperone activity. The binding of ATP and its subsequent
CC       hydrolysis by HslU are essential for unfolding of protein substrates
CC       subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of
CC       its protein substrates and unfolds these before they are guided to HslV
CC       for hydrolysis.
CC   -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on each
CC       side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV
CC       complex is dependent on binding of ATP.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
CC   -!- INDUCTION: By heat shock.
end case
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
XX
DR   Pfam; PF00004; AAA; 1; trigger=no
DR   Pfam; PF07724; AAA_2; 1; trigger=no
DR   Pfam; PF10431; ClpB_D2-small; 1; trigger=no
DR   NCBIfam; TIGR00390; HslU; 1; trigger=no
XX
KW   Cytoplasm
KW   ATP-binding
KW   Chaperone
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
KW   Stress response
end case
KW   Nucleotide-binding
XX
GO   GO:0005524; F:ATP binding
GO   GO:0036402; F:proteasome-activating activity
GO   GO:0043335; P:protein unfolding
GO   GO:0005737; C:cytoplasm
GO   GO:0009376; C:HslUV protease complex
XX
FT   From: HSLU_ECOLI (P0A6H5)
FT   BINDING         60..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-[VIC]-G-K-T-E
FT   BINDING         18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [IV]
FT   BINDING         256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: D
FT   BINDING         321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: E
FT   BINDING         393
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
XX
Size: 430-491;
Related: MF_00175;
Template: P0A6H5; P43773; P39778; Q9WYZ2;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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.
XX
# Revision 1.34 2023/06/01
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