RBCX_ANASC
ID RBCX_ANASC Reviewed; 135 AA.
AC Q44212;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=RuBisCO chaperone RbcX {ECO:0000255|HAMAP-Rule:MF_00855, ECO:0000303|PubMed:9171433};
GN Name=rbcX {ECO:0000255|HAMAP-Rule:MF_00855, ECO:0000303|PubMed:7961423};
OS Anabaena sp. (strain CA / ATCC 33047).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena;
OC unclassified Anabaena.
OX NCBI_TaxID=52271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION BY LIGHT, AND OPERON
RP STRUCTURE.
RC STRAIN=CA / ATCC 33047;
RX PubMed=7961423; DOI=10.1128/jb.176.21.6697-6706.1994;
RA Li L.A., Tabita F.R.;
RT "Transcription control of ribulose bisphosphate carboxylase/oxygenase
RT activase and adjacent genes in Anabaena species.";
RL J. Bacteriol. 176:6697-6706(1994).
RN [2]
RP FUNCTION UPON EXPRESSION IN E.COLI.
RC STRAIN=CA / ATCC 33047;
RX PubMed=9171433; DOI=10.1128/jb.179.11.3793-3796.1997;
RA Li L.A., Tabita F.R.;
RT "Maximum activity of recombinant ribulose 1,5-bisphosphate
RT carboxylase/oxygenase of Anabaena sp. strain CA requires the product of the
RT rbcX gene.";
RL J. Bacteriol. 179:3793-3796(1997).
RN [3] {ECO:0007744|PDB:2PEO}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, SUBUNIT, AND DOMAIN.
RC STRAIN=CA / ATCC 33047;
RX PubMed=17574029; DOI=10.1016/j.cell.2007.04.025;
RA Saschenbrecker S., Bracher A., Rao K.V., Rao B.V., Hartl F.U.,
RA Hayer-Hartl M.;
RT "Structure and function of RbcX, an assembly chaperone for hexadecameric
RT Rubisco.";
RL Cell 129:1189-1200(2007).
RN [4] {ECO:0007744|PDB:2WVW, ECO:0007744|PDB:3HYB}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), STRUCTURE BY ELECTRON MICROSCOPY
RP (9.00 ANGSTROMS) IN COMPLEX WITH SYNECHOCOCCUS RBCL, FUNCTION, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF 17-TYR--TYR-20 AND GLN-29.
RC STRAIN=CA / ATCC 33047;
RX PubMed=20075914; DOI=10.1038/nature08651;
RA Liu C., Young A.L., Starling-Windhof A., Bracher A., Saschenbrecker S.,
RA Rao B.V., Rao K.V., Berninghausen O., Mielke T., Hartl F.U., Beckmann R.,
RA Hayer-Hartl M.;
RT "Coupled chaperone action in folding and assembly of hexadecameric
RT Rubisco.";
RL Nature 463:197-202(2010).
RN [5] {ECO:0007744|PDB:3RG6}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH SYNECHOCOCCUS RBCL,
RP FUNCTION, AND SUBUNIT.
RC STRAIN=CA / ATCC 33047;
RX PubMed=21765418; DOI=10.1038/nsmb.2090;
RA Bracher A., Starling-Windhof A., Hartl F.U., Hayer-Hartl M.;
RT "Crystal structure of a chaperone-bound assembly intermediate of form I
RT Rubisco.";
RL Nat. Struct. Mol. Biol. 18:875-880(2011).
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 (PubMed:20075914, PubMed:21765418). {ECO:0000255|HAMAP-
CC Rule:MF_00855, ECO:0000269|PubMed:20075914,
CC ECO:0000269|PubMed:21765418}.
CC -!- FUNCTION: Required for optimal reconstitution of RuBisCO upon
CC expression of rbcL-rbcS subunits in E.coli (PubMed:9171433).
CC {ECO:0000269|PubMed:9171433}.
CC -!- SUBUNIT: Homodimer. Interacts with the exposed C-terminal peptide of
CC RbcL ('Glu-459-Asp-468'); binds 1 RbcL peptide per homodimer
CC (PubMed:17574029, PubMed:20075914, PubMed:21765418). Contacts a second
CC RbcL monomer via its peripheral polar surface (PubMed:21765418). A
CC slightly longer RbcL peptide binds to RbcX2 with a higher affinity
CC (PubMed:17574029). {ECO:0000269|PubMed:17574029,
CC ECO:0000269|PubMed:20075914, ECO:0000269|PubMed:21765418}.
CC -!- INTERACTION:
CC Q44212; P00880: cbbL; Xeno; NbExp=3; IntAct=EBI-9023244, EBI-9023246;
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00855}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00855}. Note=Most protein is
CC cytoplasmic, but some is in the carboxysome. {ECO:0000255|HAMAP-
CC Rule:MF_00855}.
CC -!- INDUCTION: Transcribed in light but much less in the dark in both
CC normal air and 1% CO(2); the nitrogen source has no effect on
CC transcription. Constitutively expressed when grown on fructose. Part of
CC the rbcL-rbcX-rbcS operon. {ECO:0000269|PubMed:7961423}.
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. {ECO:0000255|HAMAP-Rule:MF_00855,
CC ECO:0000269|PubMed:20075914, ECO:0000305|PubMed:17574029}.
CC -!- SIMILARITY: Belongs to the RbcX family. {ECO:0000255|HAMAP-
CC Rule:MF_00855}.
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DR EMBL; U05590; AAA63603.1; -; Genomic_DNA.
DR RefSeq; WP_066380855.1; NZ_LUHI01000044.1.
DR PDB; 2PEO; X-ray; 2.50 A; A/B=1-135.
DR PDB; 2WVW; EM; 9.00 A; I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-135.
DR PDB; 3HYB; X-ray; 2.30 A; A/B=1-135.
DR PDB; 3RG6; X-ray; 3.20 A; C/D/E/F=1-135.
DR PDBsum; 2PEO; -.
DR PDBsum; 2WVW; -.
DR PDBsum; 3HYB; -.
DR PDBsum; 3RG6; -.
DR AlphaFoldDB; Q44212; -.
DR SMR; Q44212; -.
DR DIP; DIP-59100N; -.
DR IntAct; Q44212; 1.
DR EvolutionaryTrace; Q44212; -.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044183; F:protein folding chaperone; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0110102; P:ribulose bisphosphate carboxylase complex assembly; IDA:UniProtKB.
DR Gene3D; 1.10.1200.210; -; 1.
DR HAMAP; MF_00855; RbcX; 1.
DR InterPro; IPR038052; Chaperonin_RbcX_sf.
DR InterPro; IPR003435; Chaperonin_RcbX.
DR InterPro; IPR046381; RbcX.
DR PANTHER; PTHR33791; PTHR33791; 1.
DR Pfam; PF02341; RbcX; 1.
DR SUPFAM; SSF158615; SSF158615; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW Carboxysome; Chaperone; Cytoplasm; Photosynthesis.
FT CHAIN 1..135
FT /note="RuBisCO chaperone RbcX"
FT /id="PRO_0000451299"
FT REGION 103..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 17..20
FT /note="YLTY->ALTA: No longer prevents RbcL-GroEL
FT association."
FT /evidence="ECO:0000269|PubMed:20075914"
FT MUTAGEN 29
FT /note="Q->A: No longer prevents RbcL-GroEL association."
FT /evidence="ECO:0000269|PubMed:20075914"
FT HELIX 3..33
FT /evidence="ECO:0007829|PDB:3HYB"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:3HYB"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:3HYB"
FT HELIX 64..81
FT /evidence="ECO:0007829|PDB:3HYB"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3HYB"
FT HELIX 85..103
FT /evidence="ECO:0007829|PDB:3HYB"
SQ SEQUENCE 135 AA; 15507 MW; 5CE932C99D632FEC CRC64;
MNLKQIAKDT AKTLQSYLTY QALRTVLAQL GETNPPLALW LHNFSAGKVQ DGEKYIEELF
LEKPDLALRI MTVREHIAEE IAEFLPEMVV TGIQQANMEK RRQHLERMTQ VSLSHPSPES
EQQQFSDPDW DNLAS
