AC   MF_00117;
DC   Protein; auto
TR   HAMAP; MF_00117; -; 1; level=0
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Names: HslO
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ID   HSLO
DE   RecName: Full=33 kDa chaperonin;
DE   AltName: Full=Heat shock protein 33 homolog;
DE            Short=HSP33;
GN   Name=hslO;
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CC   -!- FUNCTION: Redox regulated molecular chaperone. Protects both thermally
CC       unfolding and oxidatively damaged proteins from irreversible
CC       aggregation. Plays an important role in the bacterial defense system
CC       toward oxidative stress.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Under oxidizing conditions two disulfide bonds are formed
CC       involving the reactive cysteines. Under reducing conditions zinc is
CC       bound to the reactive cysteines and the protein is inactive.
CC   -!- SIMILARITY: Belongs to the HSP33 family.
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DR   Pfam; PF01430; HSP33; 1; trigger=no
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KW   Cytoplasm
KW   Chaperone
KW   Disulfide bond
KW   Redox-active center
KW   Zinc
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GO   GO:0051082; F:unfolded protein binding
GO   GO:0005737; C:cytoplasm
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FT   From: HSLO_ECOLI (P0A6Y5)
FT   DISULFID        230..232
FT                   /note="Redox-active"
FT   Condition: C-x-C
FT   DISULFID        263..266
FT                   /note="Redox-active"
FT   Condition: C-x(2)-C
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Size: 281-341;
Related: None;
Template: P0A6Y5;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Possible wrong start in AQUAE and DEIRA
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# Revision 1.20 2019/11/18
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