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|
| HAMAP annotation rule: MF_00117 |
| Accession |
MF_00117 |
| Dates |
1-JUN-2001 (Created) 9-DEC-2011 (Last updated, Version 18) |
| Protein name |
| RecName: |
Full=33 kDa chaperonin; |
| AltName: |
Full=Heat shock protein 33 homolog; Short=HSP33; |
|
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 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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 (By similarity).
SIMILARITY: Belongs to the HSP33 family.
GO:0051082; Molecular function: unfolded protein binding.
GO:0005737; Cellular component: cytoplasm.
| From: HSLO_ECOLI (P0A6Y5) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| DISULFID |
|
230 |
|
232 |
|
Redox-active (By similarity) |
|
C-x-C |
|
|
| DISULFID |
|
263 |
|
266 |
|
Redox-active (By similarity) |
|
C-x(2)-C |
|
|
| Size range: |
281-341 amino acids |
| Related UniRules: |
None |
| Template: |
P0A6Y5 (HSLO_ECOLI) |
| Scope: |
Bacteria |
| Fusion: |
Nter: None; Cter: None |
| Duplicate: |
None |
| Plasmid encoded: |
None |
| Comments: |
Possible wrong start in AQUAE and DEIRA |
View rule in raw text format (no links)