AC   MF_00248;
DC   Protein; auto
TR   HAMAP; MF_00248; -; 1; level=0
XX
Names: HslV
XX
ID   HSLV
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
DE   RecName: Full=ATP-dependent protease subunit HslV;
DE            EC=3.4.25.2;
DE   AltName: Full=Heat shock protein HslV;
else
DE   RecName: Full=ATP-dependent protease subunit HslV;
DE            EC=3.4.25.2;
end case
GN   Name=hslV;
XX
CC   -!- FUNCTION: Protease subunit of a proteasome-like degradation complex
CC       believed to be a general protein degrading machinery.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent cleavage of peptide bonds with broad
CC         specificity.; EC=3.4.25.2;
CC   -!- ACTIVITY REGULATION: Allosterically activated by HslU binding.
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 peptidase T1B family. HslV subfamily.
XX
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1; trigger=no
DR   Pfam; PF00227; Proteasome; 1; trigger=no
DR   NCBIfam; TIGR03692; ATP_dep_HslV; 1; trigger=no
XX
KW   Allosteric enzyme
KW   Cytoplasm
KW   Hydrolase
KW   Protease
case <FT:2> or <FT:3> or <FT:4>
KW   Metal-binding
KW   Sodium
end case
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
KW   Stress response
end case
KW   Threonine protease
XX
GO   GO:0008233; F:peptidase activity
GO   GO:0030163; P:protein catabolic process
GO   GO:0005737; C:cytoplasm
GO   GO:0009376; C:HslUV protease complex
XX
FT   From: HSLV_ECOLI (P0A7B8)
FT   ACT_SITE        2
FT   Condition: T
FT   BINDING         157
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT   Optional; Condition: [GAS]
FT   BINDING         160
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT   Condition: [CD]
FT   BINDING         163
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT   Condition: [TS]
XX
Size: 173-193;
Related: None;
Template: P0A7B8; P43772; P39070; Q9WYZ1;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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.
XX
# Revision 1.39 2023/06/01
//