RBCX_THEVB
ID RBCX_THEVB Reviewed; 126 AA.
AC Q8DIS6;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=RuBisCO chaperone RbcX {ECO:0000255|HAMAP-Rule:MF_00855, ECO:0000303|PubMed:19081849};
GN Name=rbcX {ECO:0000255|HAMAP-Rule:MF_00855, ECO:0000303|PubMed:19081849};
GN OrderedLocusNames=tll1505;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=19081849;
RA Tarnawski M., Gubernator B., Kolesinski P., Szczepaniak A.;
RT "Heterologous expression and initial characterization of recombinant RbcX
RT protein from Thermosynechococcus elongatus BP-1 and the role of RbcX in
RT RuBisCO assembly.";
RL Acta Biochim. Pol. 55:777-785(2008).
RN [3] {ECO:0007744|PDB:3Q20}
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF
RP CYS-103.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=21821880; DOI=10.1107/s1744309111018860;
RA Tarnawski M., Krzywda S., Bialek W., Jaskolski M., Szczepaniak A.;
RT "Structure of the RuBisCO chaperone RbcX from the thermophilic
RT cyanobacterium Thermosynechococcus elongatus.";
RL Acta Crystallogr. F Struct. Biol. Commun. 67:851-857(2011).
CC -!- FUNCTION: An RbcL-specific chaperone. Required for assembly of the
CC RbcL8 core (PubMed:19081849) (Probable). The central cleft of the RbcX
CC homodimer (RbcX2) binds the C-terminus of a 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 (By similarity). {ECO:0000250|UniProtKB:Q44212,
CC ECO:0000269|PubMed:19081849, ECO:0000305|PubMed:21821880}.
CC -!- SUBUNIT: Homodimer (PubMed:19081849, PubMed:21821880). Interacts with
CC the exposed C-terminal peptide of RbcL via its central cleft, contacts
CC a second RbcL monomer via its peripheral polar surface (By similarity).
CC {ECO:0000250|UniProtKB:Q44212, ECO:0000269|PubMed:19081849,
CC ECO:0000269|PubMed:21821880}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00855,
CC ECO:0000269|PubMed:19081849}. Cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_00855, ECO:0000269|PubMed:19081849}. Note=Most protein is
CC cytoplasmic, but some is in the carboxysome (PubMed:19081849). This
CC cyanobacterium makes beta-type carboxysomes (Probable).
CC {ECO:0000255|HAMAP-Rule:MF_00855, ECO:0000269|PubMed:19081849,
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; BA000039; BAC09057.1; -; Genomic_DNA.
DR RefSeq; NP_682295.1; NC_004113.1.
DR RefSeq; WP_011057345.1; NC_004113.1.
DR PDB; 3Q20; X-ray; 1.71 A; A/B=1-126.
DR PDBsum; 3Q20; -.
DR AlphaFoldDB; Q8DIS6; -.
DR SMR; Q8DIS6; -.
DR STRING; 197221.22295230; -.
DR EnsemblBacteria; BAC09057; BAC09057; BAC09057.
DR KEGG; tel:tll1505; -.
DR PATRIC; fig|197221.4.peg.1579; -.
DR eggNOG; ENOG50315SX; Bacteria.
DR OMA; DYLPEMV; -.
DR OrthoDB; 1698892at2; -.
DR Proteomes; UP000000440; 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..126
FT /note="RuBisCO chaperone RbcX"
FT /id="PRO_0000451304"
FT MUTAGEN 103
FT /note="C->A: Can be readily crystallized, functions in
FT RbcL8 assembly in E.coli."
FT /evidence="ECO:0000305|PubMed:21821880"
FT HELIX 3..33
FT /evidence="ECO:0007829|PDB:3Q20"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:3Q20"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:3Q20"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:3Q20"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3Q20"
FT HELIX 86..111
FT /evidence="ECO:0007829|PDB:3Q20"
SQ SEQUENCE 126 AA; 14589 MW; 1989722C24BCC176 CRC64;
MDVKHIAKQT TKTLISYLTY QAVRTVIGQL AETDPPRSLW LHQFTSQESI QDGERYLEAL
FREQPDLGFR ILTVREHLAE MVADYLPEML RAGIQQANLQ QRCQQLERMT QVSEANVENS
NLETPE
