ID   RBSC_CUPNE              Reviewed;         139 AA.
AC   P09658;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chromosomal {ECO:0000303|PubMed:2820933};
DE            Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00859};
GN   Name=cbbS {ECO:0000255|HAMAP-Rule:MF_00859};
GN   Synonyms=cbxSC, cfxSC, rbcS {ECO:0000303|PubMed:2820933};
OS   Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=106590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R;
RX   PubMed=2820933; DOI=10.1128/jb.169.10.4547-4558.1987;
RA   Andersen K., Caton J.;
RT   "Sequence analysis of the Alcaligenes eutrophus chromosomally encoded
RT   ribulose bisphosphate carboxylase large and small subunit genes and their
RT   gene products.";
RL   J. Bacteriol. 169:4547-4558(1987).
RN   [2]
RP   SEQUENCE REVISION.
RA   Andersen K.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-129 OF UNACTIVATED HOLOENYZYME,
RP   AND SUBUNIT.
RC   STRAIN=ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R;
RX   PubMed=10329167; DOI=10.1006/jmbi.1999.2701;
RA   Hansen S., Vollan V.B., Hough E., Andersen K.;
RT   "The crystal structure of rubisco from Alcaligenes eutrophus reveals a
RT   novel central eight-stranded beta-barrel formed by beta-strands from four
RT   subunits.";
RL   J. Mol. Biol. 288:609-621(1999).
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. Both reactions occur simultaneously and in competition at
CC       the same active site. Although the small subunit is not catalytic it is
CC       essential for maximal activity. {ECO:0000255|HAMAP-Rule:MF_00859}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|PubMed:10329167}.
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|PubMed:10329167}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00859}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M17744; AAC28130.1; -; Genomic_DNA.
DR   PIR; B26954; RKALSE.
DR   PDB; 1BXN; X-ray; 2.70 A; I/J/K/L=1-139.
DR   PDBsum; 1BXN; -.
DR   AlphaFoldDB; P09658; -.
DR   SMR; P09658; -.
DR   DIP; DIP-6120N; -.
DR   EvolutionaryTrace; P09658; -.
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   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; SSF55239; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calvin cycle; Carbon dioxide fixation.
FT   CHAIN           1..139
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   chromosomal"
FT                   /id="PRO_0000198607"
FT   TURN            8..10
FT                   /evidence="ECO:0007829|PDB:1BXN"
FT   HELIX           16..28
FT                   /evidence="ECO:0007829|PDB:1BXN"
FT   STRAND          32..39
FT                   /evidence="ECO:0007829|PDB:1BXN"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:1BXN"
FT   HELIX           61..74
FT                   /evidence="ECO:0007829|PDB:1BXN"
FT   STRAND          76..85
FT                   /evidence="ECO:0007829|PDB:1BXN"
FT   TURN            87..89
FT                   /evidence="ECO:0007829|PDB:1BXN"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:1BXN"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:1BXN"
FT   STRAND          110..115
FT                   /evidence="ECO:0007829|PDB:1BXN"
FT   STRAND          121..126
FT                   /evidence="ECO:0007829|PDB:1BXN"
SQ   SEQUENCE   139 AA;  16143 MW;  BDD2679F24897A1C CRC64;
     MRITQGTFSF LPELTDEQIT KQLEYCLNQG WAVGLEYTDD PHPRNTYWEM FGLPMFDLRD
     AAGILMEINN ARNTFPNHYI RVTAFDSTHT VESVVMSFIV NRPADEPGFR LVRQEEPGRT
     LRYSIESYAV QARPEGSRY