AC   MF_00580;
DC   Protein; auto
TR   HAMAP; MF_00580; -; 1; level=0
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Names: CH10
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ID   CH10
DE   RecName: Full=Co-chaperonin GroES;
DE   AltName: Full=10 kDa chaperonin;
DE   AltName: Full=Chaperonin-10;
DE            Short=Cpn10;
GN   Name=groES; Synonyms=groS;
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CC   -!- FUNCTION: Together with the chaperonin GroEL, plays an essential role
CC       in assisting protein folding. The GroEL-GroES system forms a nano-cage
CC       that allows encapsulation of the non-native substrate proteins and
CC       provides a physical environment optimized to promote and accelerate
CC       protein folding. GroES binds to the apical surface of the GroEL ring,
CC       thereby capping the opening of the GroEL channel.
CC   -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. Interacts with the
CC       chaperonin GroEL.
case <OC:Bacteria> or <OC:Archaea>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
case <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
end case
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family.
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DR   Pfam; PF00166; Cpn10; 1; trigger=no
DR   PRINTS; PR00297; CHAPERONIN10; 1; trigger=no
DR   PROSITE; PS00681; CHAPERONINS_CPN10; 1; trigger=no
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case <OC:Bacteria> or <OC:Archaea>
KW   Cytoplasm
end case
KW   Chaperone
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GO   GO:0006457; P:protein folding
case <OC:Bacteria> or <OC:Archaea>
GO   GO:0005737; C:cytoplasm
end case
case <OG:Chloroplast>
GO   GO:0009507; C:chloroplast
end case
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FT   None
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Size: 86-122;
Related: None;
Template: P0A6F9; P24301; P9WPE5;
Scope:
 Bacteria
 Archaea; Methanosarcinaceae
 Plastid
Fusion:
 Nter: None
 Cter: None
Duplicate: in BRADU, RHILO, RHIME, RHOBA, VIBCH, VIBVU
Plasmid: in RHILO, RHIME
Comments: None
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# Revision 1.38 2021/04/14
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