RBS_THEVB
ID RBS_THEVB Reviewed; 118 AA.
AC Q8DIS7;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000255|HAMAP-Rule:MF_00859};
DE Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00859};
GN Name=cbbS {ECO:0000255|HAMAP-Rule:MF_00859};
GN Synonyms=rbcS {ECO:0000255|HAMAP-Rule:MF_00859,
GN ECO:0000303|PubMed:25041569}; OrderedLocusNames=tll1504;
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 RUBISCO FOLDING AND ASSEMBLY, 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]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=25041569; DOI=10.1111/febs.12928;
RA Kolesinski P., Belusiak I., Czarnocki-Cieciura M., Szczepaniak A.;
RT "Rubisco Accumulation Factor 1 from Thermosynechococcus elongatus
RT participates in the final stages of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase assembly in Escherichia coli cells and in vitro.";
RL FEBS J. 281:3920-3932(2014).
RN [4] {ECO:0007744|PDB:2YBV, ECO:0007744|PDB:3ZXW}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), AND SUBUNIT.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RA Terlecka B., Wilhelmi V., Bialek W., Gubernator B., Szczepaniak A.,
RA Hofmann E.;
RT "Structure of Ribulose-1,5-Bisphosphate Carboxylase Oxygenase from
RT Thermosynechococcus Elongatus.";
RL Submitted (MAR-2011) to the PDB data bank.
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate in the photorespiration process. Both reactions occur
CC simultaneously and in competition at the same active site. Although the
CC small subunit is not catalytic it is essential for maximal activity.
CC {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|PubMed:25041569}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|PubMed:25041569,
CC ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00859,
CC ECO:0000305|PubMed:25041569}. Note=This cyanobacterium makes beta-type
CC carboxysomes. {ECO:0000305}.
CC -!- MISCELLANEOUS: RuBisCO folding and assembly commences when the nascent
CC large subunit folds with the help of chaperonin GroEL-GroES. Both RbcX
CC and Raf1 help folded RbcL release from the chaperonin and dimerize
CC (Probable). Dimeric Raf1 binds to RbcL(2) leading to an RbcL8-Raf1(8)
CC complex. RbcS displaces Raf1, resulting in holoenzyme formation (By
CC similarity). {ECO:0000250|UniProtKB:P00879,
CC ECO:0000305|PubMed:19081849, ECO:0000305|PubMed:25041569}.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00859}.
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DR EMBL; BA000039; BAC09056.1; -; Genomic_DNA.
DR RefSeq; NP_682294.1; NC_004113.1.
DR RefSeq; WP_011057344.1; NC_004113.1.
DR PDB; 2YBV; X-ray; 2.30 A; B/D/F/H/J/L/N/P=1-118.
DR PDB; 3ZXW; X-ray; 2.10 A; B/D/F/H=1-118.
DR PDBsum; 2YBV; -.
DR PDBsum; 3ZXW; -.
DR AlphaFoldDB; Q8DIS7; -.
DR SMR; Q8DIS7; -.
DR STRING; 197221.22295229; -.
DR EnsemblBacteria; BAC09056; BAC09056; BAC09056.
DR KEGG; tel:tll1504; -.
DR PATRIC; fig|197221.4.peg.1578; -.
DR eggNOG; COG4451; Bacteria.
DR OMA; KQCQVLS; -.
DR OrthoDB; 1708389at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR CDD; cd03527; RuBisCO_small; 1.
DR Gene3D; 3.30.190.10; -; 1.
DR HAMAP; MF_00859; RuBisCO_S_bact; 1.
DR InterPro; IPR024681; RuBisCO_ssu.
DR InterPro; IPR000894; RuBisCO_ssu_dom.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR PANTHER; PTHR31262; PTHR31262; 1.
DR Pfam; PF00101; RuBisCO_small; 1.
DR PRINTS; PR00152; RUBISCOSMALL.
DR SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; SSF55239; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Calvin cycle;
KW Carbon dioxide fixation; Carboxysome; Photorespiration; Photosynthesis;
KW Reference proteome.
FT CHAIN 1..118
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /id="PRO_0000451581"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:2YBV"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:3ZXW"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:3ZXW"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:3ZXW"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:3ZXW"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:3ZXW"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:3ZXW"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:3ZXW"
SQ SEQUENCE 118 AA; 13987 MW; FA8A39F5A519085E CRC64;
MKTLPKERRY ETFSYLPPLS DAQIARQIQY AIDQGYHPCV EFNETSNAEI RYWTMWKLPL
FNCTNAQDVL NEVQQCRSEY PNCFIRVVAF DNIKQCQVMS FIVYKPNQAN SGYSGYRY
