AC   MF_00855;
DC   Protein; auto
TR   HAMAP; MF_00855; -; 1; level=0
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Names: RbcX
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ID   RBCX
DE   RecName: Full=RuBisCO chaperone RbcX;
GN   Name=rbcX;
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CC   -!- FUNCTION: An RbcL-specific chaperone. The central cleft of the RbcX
CC       homodimer (RbcX2) binds the C-terminus of an RbcL monomer, stabilizing
CC       the C-terminus and probably preventing its reassociation with
CC       chaperonin GroEL-ES. At the same time the peripheral region of RbcX2
CC       binds a second RbcL monomer, bridging the RbcL homodimers in the
CC       correct orientation. The RbcX2(2)-bound RbcL dimers then assemble into
CC       the RbcL8 core (RbcL8-(RbcX2)8). RbcS binding triggers the release of
CC       RbcX2.
CC   -!- SUBUNIT: Homodimer. Interacts with the exposed C-terminal peptide of
CC       RbcL via its central cleft, contacts a second RbcL monomer via its
CC       peripheral polar surface.
CC   -!- SUBCELLULAR LOCATION: Carboxysome. Cytoplasm. Note=Most protein is
CC       cytoplasmic, but some is in the carboxysome.
CC   -!- DOMAIN: The homodimer has 2 functional domains, a central cleft
CC       essential for production of soluble RbcL in which the RbcL peptide
CC       binds, and a polar surface which plays a role in correct RbcL subunit
CC       arrangement.
CC   -!- SIMILARITY: Belongs to the RbcX family.
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DR   Pfam; PF02341; RcbX; 1; trigger=no
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KW   Carbon dioxide fixation
KW   Carboxysome
KW   Chaperone
KW   Cytoplasm
KW   Photosynthesis
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GO   GO:0015977; P:carbon fixation
GO   GO:0031470; C:carboxysome
GO   GO:0005737; C:cytoplasm
GO   GO:0110102; P:ribulose bisphosphate carboxylase complex assembly
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FT   None
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Size: 120-183;
Related: None;
Template: Q44212; Q44177;
Scope:
 Bacteria; Cyanobacteriota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.4 2023/02/17
//