ID   RBSP_CUPNH              Reviewed;         139 AA.
AC   Q59102; Q59103;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, plasmid {ECO:0000303|PubMed:7543477};
DE            Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00859};
GN   Name=cbbS {ECO:0000255|HAMAP-Rule:MF_00859};
GN   Synonyms=cbbSP, cbxSP, cfxSP, rbcS; OrderedLocusNames=PHG426;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OG   Plasmid megaplasmid pHG1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7543477; DOI=10.1128/jb.177.15.4442-4450.1995;
RA   Kusian B., Bednarski R., Husemann M., Bowien B.;
RT   "Characterization of the duplicate ribulose-1,5-bisphosphate carboxylase
RT   genes and cbb promoters of Alcaligenes eutrophus.";
RL   J. Bacteriol. 177:4442-4450(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA   Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT   "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT   encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL   J. Mol. Biol. 332:369-383(2003).
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}.
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}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00859}.
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DR   EMBL; U20584; AAA83746.1; -; Genomic_DNA.
DR   EMBL; U20585; AAA83748.1; -; Genomic_DNA.
DR   EMBL; AY305378; AAP86175.1; -; Genomic_DNA.
DR   PIR; I39558; I39558.
DR   PIR; I39560; I39560.
DR   RefSeq; WP_011154338.1; NZ_CP039289.1.
DR   AlphaFoldDB; Q59102; -.
DR   SMR; Q59102; -.
DR   STRING; 381666.H16_B1394; -.
DR   EnsemblBacteria; AAP86175; AAP86175; PHG426.
DR   GeneID; 39976389; -.
DR   KEGG; reh:PHG426; -.
DR   PATRIC; fig|381666.6.peg.354; -.
DR   eggNOG; COG4451; Bacteria.
DR   HOGENOM; CLU_098114_2_0_4; -.
DR   OMA; VYIINQG; -.
DR   OrthoDB; 1708389at2; -.
DR   Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Plasmid; Reference proteome.
FT   CHAIN           1..139
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   plasmid"
FT                   /id="PRO_0000198608"
FT   CONFLICT        105
FT                   /note="D -> E (in Ref. 1; AAA83746)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="I -> M (in Ref. 1; AAA83746)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   139 AA;  15985 MW;  96B373592929C454 CRC64;
     MRITQGTFSF LPDLTDAQIT SQLEYCLNQG WAVGIEYTDD PHPRNTYWEM FGLPMFDLRD
     AAGILLEINN ARSTFPNHYI RVTAFDSTHT VESVVMSFIV NRPADEPGFR LVRQEEPGRT
     IRYSIESYAV QARPEGSRY