HAMAP rule MF_00249
General rule information
[?]
| PURL | https://purl.expasy.org/hamap/rule/MF_00249 |
| Accession | MF_00249 |
| Dates | 28-FEB-2005 (Created)
01-JUN-2023 (Last updated, Version 25) |
| Name | HslU |
| Scope(s) |
Bacteria |
| Template(s) | P0A6H5; P43773; P39778; Q9WYZ2; [ Recover all ] |
| Triggered by |
HAMAP; MF_00249 (Get profile general information and statistics) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
| 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 | Name=hslU; |
Comments
[?]
| 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. |
| 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 ClpX chaperone family. HslU subfamily. |
Keywords
[?]
| Cytoplasm | |
| ATP-binding | |
| Chaperone | |
| case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella> | |
| Stress response | |
| end case | |
| Nucleotide-binding | |
Gene Ontology
[?]
| GO:0005524; Molecular function:ATP binding |
| GO:0036402; Molecular function:proteasome-activating activity |
| GO:0043335; Biological process:protein unfolding |
| GO:0005737; Cellular component:cytoplasm |
| GO:0009376; Cellular component:HslUV protease complex |
Cross-references
[?]
| Pfam | PF00004; AAA; 1; |
| Pfam | PF07724; AAA_2; 1; |
| Pfam | PF10431; ClpB_D2-small; 1; |
| NCBIfam | TIGR00390; HslU; 1; |
Features
[?]
| From: HSLU_ECOLI (P0A6H5) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 60 | 65 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G-[VIC]-G-K-T-E | ||||||||
| BINDING | 18 | 18 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[IV] | ||||||||
| BINDING | 256 | 256 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
D | ||||||||
| BINDING | 321 | 321 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
E | ||||||||
| BINDING | 393 | 393 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R | ||||||||
Additional information
[?]
| Size range | 430-491 amino acids |
| Related rules |
MF_00175 |
| Fusion | Nter: None Cter: 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. |