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Annotation rule MF_00248
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General rule information [?]

Accession MF_00248
Dates 1-JUN-2001 (Created)
18-NOV-2019 (Last updated, Version 36)
Name HslV
Templates P0A7B8 (HSLV_ECOLI); P43772 (HSLV_HAEIN); P39070 (CLPQ_BACSU); Q9WYZ1 (HSLV_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 subunit HslV;
AltName: Full=Heat shock protein HslV;
Protein name
RecName: Full=ATP-dependent protease subunit HslV;
end case
Gene name

Comments [?]

Function Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic activity Reaction=ATP-dependent cleavage of peptide bonds with broad specificity.; EC=;
Activity regulation Allosterically activated by HslU binding.
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 peptidase T1B family. HslV subfamily.

Keywords [?]

case <FT:2> or <FT:3> or <FT:4>
end case
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
end case

Gene Ontology [?]

GO:0008233; Molecular function: peptidase activity.
GO:0030163; Biological process: protein catabolic process.
GO:0005737; Cellular component: cytoplasm.
GO:0009376; Cellular component: HslUV protease complex.

Cross-references [?]

Pfam PF00227; Proteasome; 1;
TIGRFAMs TIGR03692; ATP_dep_HslV; 1;

Features [?]

Key     From     To       Description   Tag   Condition   FTGroup
ACT_SITE     2     2             T  
METAL (Optional)     157     157       Sodium; via carbonyl oxygen     [GAS]  
METAL     160     160       Sodium; via carbonyl oxygen     [CD]  
METAL     163     163       Sodium; via carbonyl oxygen     [TS]  

Additional information [?]

Size range 173-193 amino acids
Related rules None
Fusion None
Comments The ATPase subunit of the HslUV complex is described in MF_00249. The family member in B.subtilis (ClpQ) was shown to be a serine protease (EC=3.4.21.-) and not a threonine protease (EC=3.4.25.-). The N-terminus with the active site Ser is conserved only in some bacilli. The threonine (or serine) active site should be at the first position in the mature protein, so each protein should contain a FT INIT_MET or FT PROPEP, but this is not currently possible to make the rule manage this.