HAMAP rule MF_00117
General rule information
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| Accession | MF_00117 |
| Dates | 1-JUN-2001 (Created)
18-NOV-2019 (Last updated, Version 20) |
| Name | HslO |
| Scope(s) |
Bacteria |
| Template(s) | P0A6Y5 (HSLO_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_00117 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | HSLO |
| Protein name | RecName: Full=33 kDa chaperonin; AltName: Full=Heat shock protein 33 homolog; Short=HSP33; |
| Gene name | Name=hslO; |
Comments
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| FUNCTION | Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| PTM | Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive. |
| SIMILARITY | Belongs to the HSP33 family. |
Keywords
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Gene Ontology
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| GO:0051082; Molecular function:unfolded protein binding |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| Pfam | PF01430; HSP33; 1; |
Features
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| From: HSLO_ECOLI (P0A6Y5) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DISULFID | 230 | 232 | /note="Redox-active" | C-x-C | ||||||||
| DISULFID | 263 | 266 | /note="Redox-active" | C-x(2)-C | ||||||||
Additional information
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| Size range | 281-341 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | Possible wrong start in AQUAE and DEIRA |