RBCX_SYNY3
ID RBCX_SYNY3 Reviewed; 138 AA.
AC Q55670;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=RuBisCO chaperone RbcX {ECO:0000255|HAMAP-Rule:MF_00855, ECO:0000303|PubMed:17881829};
GN Name=rbcX {ECO:0000255|HAMAP-Rule:MF_00855, ECO:0000303|PubMed:17881829};
GN OrderedLocusNames=slr0011;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2] {ECO:0007744|PDB:2PY8}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 3-138, AND SUBUNIT.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=17881829; DOI=10.1107/s090744490704228x;
RA Tanaka S., Sawaya M.R., Kerfeld C.A., Yeates T.O.;
RT "Structure of the RuBisCO chaperone RbcX from Synechocystis sp. PCC6803.";
RL Acta Crystallogr. D 63:1109-1112(2007).
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 -!- SUBUNIT: Homodimer (PubMed:17881829). Interacts with the exposed C-
CC terminal peptide of RbcL via its central cleft, contacts a second RbcL
CC monomer via its peripheral polar surface (By similarity).
CC {ECO:0000250|UniProtKB:Q44212, ECO:0000269|PubMed:17881829}.
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 -!- 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; BA000022; BAA10191.1; -; Genomic_DNA.
DR PIR; S76339; S76339.
DR PDB; 2PY8; X-ray; 2.45 A; A/B/C/D=3-138.
DR PDBsum; 2PY8; -.
DR AlphaFoldDB; Q55670; -.
DR SMR; Q55670; -.
DR IntAct; Q55670; 13.
DR STRING; 1148.1001564; -.
DR PaxDb; Q55670; -.
DR EnsemblBacteria; BAA10191; BAA10191; BAA10191.
DR KEGG; syn:slr0011; -.
DR eggNOG; ENOG50315SX; Bacteria.
DR InParanoid; Q55670; -.
DR OMA; DYLPEMV; -.
DR EvolutionaryTrace; Q55670; -.
DR Proteomes; UP000001425; 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 3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW Carboxysome; Chaperone; Cytoplasm; Photosynthesis; Reference proteome.
FT CHAIN 1..138
FT /note="RuBisCO chaperone RbcX"
FT /id="PRO_0000451303"
FT REGION 118..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 5..35
FT /evidence="ECO:0007829|PDB:2PY8"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:2PY8"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:2PY8"
FT HELIX 67..84
FT /evidence="ECO:0007829|PDB:2PY8"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2PY8"
FT HELIX 88..119
FT /evidence="ECO:0007829|PDB:2PY8"
SQ SEQUENCE 138 AA; 15592 MW; 96E64FF576B25252 CRC64;
MFMQTKHIAQ ATVKVLQSYL TYQAVLRIQS ELGETNPPQA IWLNQYLASH SIQNGETFLT
ELLDENKELV LRILAVREDI AESVLDFLPG MTRNSLAESN IAHRRHLLER LTRTVAEVDN
FPSETSNGES NNNDSPPS
