HAMAP rule MF_00855

Accession	MF_00855
Dates	20-AUG-2020 (Created) 17-FEB-2023 (Last updated, Version 4)

Name

RbcX

Scope

Bacteria; Cyanobacteriota

Templates

Q44212 (RBCX_ANASC); Q44177 (RBCX_SYNP2): [Recover all]

Triggered by

HAMAP; MF_00855 (Get profile general information and statistics)

Identifier

RBCX

Protein name

RecName: Full=RuBisCO chaperone RbcX;

Gene name

rbcX

Function	An 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.
Subunit	Homodimer. Interacts with the exposed C-terminal peptide of RbcL via its central cleft, contacts a second RbcL monomer via its peripheral polar surface.
Subcellular location	Carboxysome. Cytoplasm. Note=Most protein is cytoplasmic, but some is in the carboxysome.
Domain	The 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.
Similarity	Belongs to the RbcX family.

Carbon dioxide fixation
Carboxysome
Chaperone
Cytoplasm
Photosynthesis

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.

Pfam	PF02341; RcbX; 1;

Size range	120-183 amino acids
Related rules	None
Fusion	None

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