ID   RBS_ALVHS               Reviewed;         121 AA.
AC   P24682;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 78.
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}; Synonyms=rbcS;
OS   Alvinoconcha hessleri symbiotic bacterium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=2326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2247456; DOI=10.1073/pnas.87.22.8850;
RA   Stein J.L., Haygood M., Felbeck H.;
RT   "Nucleotide sequence and expression of a deep-sea ribulose-1,5-bisphosphate
RT   carboxylase gene cloned from a chemoautotrophic bacterial endosymbiont.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8850-8854(1990).
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; M34536; AAA27388.1; -; Genomic_DNA.
DR   PIR; B38262; RKJVSA.
DR   AlphaFoldDB; P24682; -.
DR   SMR; P24682; -.
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.
FT   CHAIN           1..121
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /id="PRO_0000198609"
SQ   SEQUENCE   121 AA;  13857 MW;  FC16F98CC150D67D CRC64;
     MSEIQDYNSS VSDPSSRKFE TFSYLPELGV EKIRKQVEYI VSKGWNPAVE HTEPENAFDH
     YWYMWKLPMF GETDVDAILA EAEACHKAHP SHHVRLIGYD NYAQSQGTAM VIFRGPISAK
     C