RBCX_NOSS1
ID RBCX_NOSS1 Reviewed; 132 AA.
AC O86418;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=RuBisCO chaperone RbcX {ECO:0000255|HAMAP-Rule:MF_00855};
GN Name=rbcX {ECO:0000255|HAMAP-Rule:MF_00855}; OrderedLocusNames=alr1525;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2]
RP FUNCTION IN E.COLI.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=8472962; DOI=10.1016/0378-1119(93)90593-r;
RA Larimer F.W., Soper T.S.;
RT "Overproduction of Anabaena 7120 ribulose-bisphosphate
RT carboxylase/oxygenase in Escherichia coli.";
RL Gene 126:85-92(1993).
RN [3]
RP DISCUSSION OF FUNCTION.
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 FUNCTION, AND SUBUNIT.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=32451445; DOI=10.1038/s41477-020-0665-8;
RA Xia L.Y., Jiang Y.L., Kong W.W., Sun H., Li W.F., Chen Y., Zhou C.Z.;
RT "Molecular basis for the assembly of RuBisCO assisted by the chaperone
RT Raf1.";
RL Nat. Plants 6:708-717(2020).
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. {ECO:0000255|HAMAP-Rule:MF_00855}.
CC -!- FUNCTION: When rbcL-rbcX-rbcS or rbcL-rbcS were overexpressed in E.coli
CC no change in reconstituted RuBisCO activity was observed, which
CC suggests RbcX plays no role in RuBisCO assembly in this system
CC (PubMed:8472962). However in PubMed:8472962 E.coli chaperones groL and
CC groS were also overexpressed, which may compensate for lack of rbcX
CC (Probable). {ECO:0000269|PubMed:8472962, ECO:0000305|PubMed:15564522}.
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 (By similarity). RbcX and Raf1 can bind
CC simultaneously to RbcL (PubMed:32451445). {ECO:0000255|HAMAP-
CC Rule:MF_00855, ECO:0000269|PubMed:32451445}.
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 -!- 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 -!- SIMILARITY: Belongs to the RbcX family. {ECO:0000255|HAMAP-
CC Rule:MF_00855}.
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DR EMBL; BA000019; BAB77891.1; -; Genomic_DNA.
DR PIR; AG1996; AG1996.
DR RefSeq; WP_010995694.1; NZ_RSCN01000022.1.
DR AlphaFoldDB; O86418; -.
DR SMR; O86418; -.
DR STRING; 103690.17135345; -.
DR EnsemblBacteria; BAB77891; BAB77891; BAB77891.
DR GeneID; 58726708; -.
DR KEGG; ana:alr1525; -.
DR eggNOG; ENOG50315SX; Bacteria.
DR OMA; DYLPEMV; -.
DR OrthoDB; 1698892at2; -.
DR Proteomes; UP000002483; 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: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; IEA:InterPro.
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 Bacterial microcompartment; Carbon dioxide fixation; Carboxysome;
KW Chaperone; Cytoplasm; Photosynthesis; Reference proteome.
FT CHAIN 1..132
FT /note="RuBisCO chaperone RbcX"
FT /id="PRO_0000451582"
FT REGION 99..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 132 AA; 15191 MW; 69740AE5B44DC5BE CRC64;
MNLKQIAKDT AKTLQSYLTY QALMTVLAQL GETNPPLALW LHTFSVGKVQ DGEAYVKELF
REQPDLALRI MTVREHIAEE VAEFLPEMVR SGIQQANMEQ RRQHLERMTH LSLSNPSPES
EQQTISDTDW DH
