RBCX_SYNP2
ID RBCX_SYNP2 Reviewed; 134 AA.
AC Q44177;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=RuBisCO chaperone RbcX {ECO:0000255|HAMAP-Rule:MF_00855, ECO:0000303|PubMed:15564522};
GN Name=rbcX {ECO:0000255|HAMAP-Rule:MF_00855, ECO:0000303|PubMed:15564522};
GN Synonyms=orf134 {ECO:0000303|Ref.1}; OrderedLocusNames=SYNPCC7002_A1797;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Akiyama H., Kanai S., Hirano M., Sugimoto M., Kiyohara M.;
RT "Cloning and characterization of RubisCO large subunit and small subunit
RT from Synechococcus sp. PCC7002.";
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, EXPRESSION IN E.COLI, AND FRAMESHIFT MUTATION.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX PubMed=15564522; DOI=10.1093/pcp/pch160;
RA Onizuka T., Endo S., Akiyama H., Kanai S., Hirano M., Yokota A., Tanaka S.,
RA Miyasaka H.;
RT "The rbcX gene product promotes the production and assembly of ribulose-
RT 1,5-bisphosphate carboxylase/oxygenase of Synechococcus sp. PCC7002 in
RT Escherichia coli.";
RL Plant Cell Physiol. 45:1390-1395(2004).
RN [4]
RP SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
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:2PEI, ECO:0007744|PDB:2PEJ, ECO:0007744|PDB:2PEK, ECO:0007744|PDB:2PEM, ECO:0007744|PDB:2PEN, ECO:0007744|PDB:2PEQ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (2.95
RP ANGSTROMS) IN COMPLEX WITH AN RBCL PEPTIDE, FUNCTION, EXPRESSION IN E.COLI,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF 17-TYR--TYR-20; TYR-17; TYR-20; GLN-29;
RP GLU-32; THR-33; PRO-35; ARG-70; VAL-74; ARG-102 AND 110-THR--GLU-134.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
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 [6] {ECO:0007744|PDB:2Z44, ECO:0007744|PDB:2Z45, ECO:0007744|PDB:2Z46}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Tomimoto Y., Ihara K., Onizuka T., Kanai S., Ashida H., Yokota A.,
RA Tanaka S., Miyasaka H., Yamada Y., Kato R., Wakatsuki S.;
RT "Crystal Structure of ORF134.";
RL Submitted (JUN-2007) to the PDB data bank.
CC -!- FUNCTION: An RbcL-specific chaperone. Required for assembly of the
CC RbcL8 core, acting downstream of the major chaperonin (GroEL-GroES).
CC Acts on newly folded RbcL, has a transient dynamic interaction with
CC RbcL and is eventually displaced by RbcS (PubMed:17574029). The central
CC cleft of the RbcX homodimer (RbcX2) binds the C-terminus of an RbcL
CC monomer, stabilizing the C-terminus and probably preventing its
CC reassociation with chaperonin GroEL-ES. At the same time the peripheral
CC region of RbcX2 binds a second RbcL monomer, bridging the RbcL
CC homodimers in the correct orientation. The RbcX2(2)-bound RbcL dimers
CC then assemble into the RbcL8 core (RbcL8-(RbcX2)8). RbcS binding
CC triggers the release of RbcX2 (By similarity). Required for optimal
CC reconstitution of RuBisCO into its RbcL8S8 holoenzyme form upon
CC expression of rbcL-rbcS subunits in E.coli, and probably also in situ.
CC A frameshift mutation that replaces half the protein reduces
CC accumulation of both RbcL and RbcS subunits and halves activity of
CC RuBisCO in situ and in E.coli (PubMed:15564522).
CC {ECO:0000250|UniProtKB:Q44212, ECO:0000269|PubMed:15564522,
CC ECO:0000269|PubMed:17574029}.
CC -!- SUBUNIT: Homodimer (RbcX2) (PubMed:17574029, Ref.6). Interacts with the
CC exposed C-terminal peptide of RbcL ('Glu-459-Asp-468'); binds 2 RbcL
CC peptides per RbcX2, stapling them into an RbcL2 dimer. A slightly
CC longer peptide binds with a higher affinity, but no long-term stable
CC interaction with RbcL is detected (PubMed:17574029, PubMed:20075914).
CC Contacts a second RbcL monomer via its peripheral polar surface (By
CC similarity). {ECO:0000250|UniProtKB:Q44212,
CC ECO:0000269|PubMed:17574029, ECO:0000269|PubMed:20075914,
CC ECO:0000269|Ref.6}.
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. This cyanobacterium makes
CC beta-type carboxysomes (Probable). {ECO:0000255|HAMAP-Rule:MF_00855,
CC ECO:0000305}.
CC -!- INDUCTION: Part of the rbcL-rbcX-rbcS operon. {ECO:0000305}.
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:17574029, ECO:0000269|PubMed:20075914}.
CC -!- SIMILARITY: Belongs to the RbcX family. {ECO:0000255|HAMAP-
CC Rule:MF_00855}.
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DR EMBL; CP000951; ACA99785.1; -; Genomic_DNA.
DR EMBL; D13971; BAA03077.1; -; Genomic_DNA.
DR RefSeq; WP_012307408.1; NC_010475.1.
DR PDB; 2PEI; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-109.
DR PDB; 2PEJ; X-ray; 3.40 A; A/B/C/D/E/F=1-134.
DR PDB; 2PEK; X-ray; 3.10 A; A/B/C/D/E/F=1-134.
DR PDB; 2PEM; X-ray; 2.95 A; A/B/C/D/E/F=1-134.
DR PDB; 2PEN; X-ray; 2.80 A; A/B/C/D/E/F=1-134.
DR PDB; 2PEQ; X-ray; 1.90 A; A/B=1-134.
DR PDB; 2Z44; X-ray; 2.50 A; A=1-134.
DR PDB; 2Z45; X-ray; 2.15 A; A/B=1-134.
DR PDB; 2Z46; X-ray; 2.97 A; A/B/C/D/E/F=1-134.
DR PDBsum; 2PEI; -.
DR PDBsum; 2PEJ; -.
DR PDBsum; 2PEK; -.
DR PDBsum; 2PEM; -.
DR PDBsum; 2PEN; -.
DR PDBsum; 2PEQ; -.
DR PDBsum; 2Z44; -.
DR PDBsum; 2Z45; -.
DR PDBsum; 2Z46; -.
DR AlphaFoldDB; Q44177; -.
DR SMR; Q44177; -.
DR STRING; 32049.SYNPCC7002_A1797; -.
DR EnsemblBacteria; ACA99785; ACA99785; SYNPCC7002_A1797.
DR KEGG; syp:SYNPCC7002_A1797; -.
DR eggNOG; ENOG50315SX; Bacteria.
DR HOGENOM; CLU_129346_0_0_3; -.
DR OMA; DYLPEMV; -.
DR EvolutionaryTrace; Q44177; -.
DR Proteomes; UP000001688; Chromosome.
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; IMP: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; IMP:UniProtKB.
DR DisProt; DP02968; -.
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; Reference proteome.
FT CHAIN 1..134
FT /note="RuBisCO chaperone RbcX"
FT /id="PRO_0000451301"
FT REGION 97..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 17..20
FT /note="YLTY->ALTL: No longer assembles RbcL8, no active
FT RuBisCO formed, no change in crystal structure."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 17
FT /note="Y->A: Assembles about 50% RbcL8."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 20
FT /note="Y->A,L: Assembles about 50% RbcL8."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 29
FT /note="Q->A: No longer assembles RbcL8, forms a larger
FT misassembled complex, no active RuBisCO formed."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 32
FT /note="E->A: No longer assembles RbcL8, no active RuBisCO
FT formed."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 33
FT /note="T->A: Assembles about 50% RbcL8."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 35
FT /note="P->A: Assembles about 50% RbcL8."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 70
FT /note="R->A: No longer assembles RbcL8, no active RuBisCO
FT formed."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 74
FT /note="V->A: Assembles about 50% RbcL8."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 102
FT /note="R->A: No longer assembles RbcL8, no active RuBisCO
FT formed."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 110..134
FT /note="Missing: Still assembles RbcL8 core."
FT /evidence="ECO:0000269|PubMed:17574029"
FT HELIX 3..33
FT /evidence="ECO:0007829|PDB:2PEQ"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:2PEQ"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:2PEQ"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:2PEQ"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2PEQ"
FT HELIX 86..108
FT /evidence="ECO:0007829|PDB:2PEQ"
SQ SEQUENCE 134 AA; 15269 MW; A11F42E96F424988 CRC64;
MEFKKVAKET AITLQSYLTY QAVRLISQQL SETNPGQAIW LGEFSKRHPI QESDLYLEAM
MLENKELVLR ILTVRENLAE GVLEFLPEMV LSQIKQSNGN HRRSLLERLT QVDSSSTDQT
EPNPGESDTS EDSE
