ID   RBS_THIDA               Reviewed;         118 AA.
AC   Q56260; Q3SFN0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 114.
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   OrderedLocusNames=Tbd_2623;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8550452; DOI=10.1128/jb.178.2.347-356.1996;
RA   Hernandez J.M., Baker S.H., Lorbach S.C., Shively J.M., Tabita F.R.;
RT   "Deduced amino acid sequence, functional expression, and unique enzymatic
RT   properties of the form I and form II ribulose bisphosphate
RT   carboxylase/oxygenase from the chemoautotrophic bacterium Thiobacillus
RT   denitrificans.";
RL   J. Bacteriol. 178:347-356(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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; L42940; AAB70698.1; -; Genomic_DNA.
DR   EMBL; CP000116; AAZ98576.1; -; Genomic_DNA.
DR   RefSeq; WP_011313135.1; NC_007404.1.
DR   AlphaFoldDB; Q56260; -.
DR   SMR; Q56260; -.
DR   STRING; 292415.Tbd_2623; -.
DR   KEGG; tbd:Tbd_2623; -.
DR   eggNOG; COG4451; Bacteria.
DR   HOGENOM; CLU_098114_2_0_4; -.
DR   OrthoDB; 9788955at2; -.
DR   Proteomes; UP000008291; Chromosome.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd03527; RuBisCO_small; 1.
DR   Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 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; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; RuBisCO, small subunit; 1.
PE   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Reference proteome.
FT   CHAIN           1..118
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /id="PRO_0000198628"
SQ   SEQUENCE   118 AA;  13608 MW;  4A45CFDA4FC98F63 CRC64;
     MSEVMDYKSR LSDPASRKFE TFSYLPAMNA ADIRKQVEYL VSKGWNPAIE HTEPEHLMDS
     YWYMWKLPMF GETDIDRILG EAEACHKANP NNHVRLVGYD NFAQSQGAAM VIYRGKTV
//