HAMAP rule MF_00248
General rule information
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| Accession | MF_00248 |
| Dates | 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 39) |
| Name | HslV |
| Scope(s) |
Bacteria |
| Template(s) | P0A7B8 (HSLV_ECOLI); P43772 (HSLV_HAEIN); P39070 (CLPQ_BACSU); Q9WYZ1 (HSLV_THEMA); [ Recover all ] |
| Triggered by |
HAMAP; MF_00248 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | HSLV |
| case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella> | |
| Protein name | RecName: Full=ATP-dependent protease subunit HslV; EC=3.4.25.2; AltName: Full=Heat shock protein HslV; |
| else | |
| Protein name | RecName: Full=ATP-dependent protease subunit HslV; EC=3.4.25.2; |
| end case | |
| Gene name | Name=hslV; |
Comments
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| 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=3.4.25.2; |
| 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
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| Allosteric enzyme | |
| Cytoplasm | |
| Hydrolase | |
| Protease | |
| case <FT:2> or <FT:3> or <FT:4> | |
| Metal-binding | |
| Sodium | |
| end case | |
| case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella> | |
| Stress response | |
| end case | |
| Threonine protease | |
Gene Ontology
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| 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
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| PROSITE | PS51476; PROTEASOME_BETA_2; 1; |
| Pfam | PF00227; Proteasome; 1; |
| NCBIfam | TIGR03692; ATP_dep_HslV; 1; |
Features
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| From: HSLV_ECOLI (P0A7B8) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 2 | 2 | T | |||||||||
| BINDING | 157 | 157 | /ligand="Na(+)" /ligand_id="ChEBI:CHEBI:29101" |
[GAS] | ||||||||
| BINDING | 160 | 160 | /ligand="Na(+)" /ligand_id="ChEBI:CHEBI:29101" |
[CD] | ||||||||
| BINDING | 163 | 163 | /ligand="Na(+)" /ligand_id="ChEBI:CHEBI:29101" |
[TS] | ||||||||
Additional information
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| Size range | 173-193 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: 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. |