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HAMAP rule MF_00855

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General rule information [?]

Accession MF_00855
Dates 20-AUG-2020 (Created)
17-FEB-2023 (Last updated, Version 4)
Name RbcX
Scope(s) Bacteria
Template(s) Q44212 (RBCX_ANASC); Q44177 (RBCX_PICP2); [ Recover all ]
Triggered by HAMAP; MF_00855 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier RBCX
Protein name RecName: Full=RuBisCO chaperone RbcX;
Gene name Name=rbcX;

Comments [?]

FUNCTIONAn RbcL-specific chaperone. The central cleft of the RbcX homodimer (RbcX2) binds the C-terminus of an RbcL monomer, stabilizing the C-terminus and probably preventing its reassociation with chaperonin GroEL-ES. At the same time the peripheral region of RbcX2 binds a second RbcL monomer, bridging the RbcL homodimers in the correct orientation. The RbcX2(2)-bound RbcL dimers then assemble into the RbcL8 core (RbcL8-(RbcX2)8). RbcS binding triggers the release of RbcX2.
SUBUNITHomodimer. Interacts with the exposed C-terminal peptide of RbcL via its central cleft, contacts a second RbcL monomer via its peripheral polar surface.
SUBCELLULAR LOCATIONCarboxysome. Cytoplasm. Note=Most protein is cytoplasmic, but some is in the carboxysome.
DOMAINThe homodimer has 2 functional domains, a central cleft essential for production of soluble RbcL in which the RbcL peptide binds, and a polar surface which plays a role in correct RbcL subunit arrangement.
SIMILARITYBelongs to the RbcX family.

Keywords [?]

Gene Ontology [?]

GO:0015977; Biological process:carbon fixation
GO:0031470; Cellular component:carboxysome
GO:0005737; Cellular component:cytoplasm
GO:0110102; Biological process:ribulose bisphosphate carboxylase complex assembly

Cross-references [?]

Pfam PF02341; RcbX; 1;

Features [?]

Additional information [?]

Size range 120-183 amino acids
Related rules None
Fusion Nter: None Cter: None

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