ID   RBS2_BRANA              Reviewed;         181 AA.
AC   P27985;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 2 {ECO:0000255|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit 2 {ECO:0000255|HAMAP-Rule:MF_00860};
DE   Flags: Precursor;
GN   Name=RBCS2 {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS F1;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Westar;
RX   PubMed=1863768; DOI=10.1007/bf00016068;
RA   Nantel A.M., Lafleur F., Boivin R., Baszczynski C.L., Bellemare G.;
RT   "Promoter for a Brassica napus ribulose bisphosphate carboxylase/oxygenase
RT   small subunit gene binds multiple nuclear factors and contains a negative-
RT   strand open reading frame encoding a putative transmembrane protein.";
RL   Plant Mol. Biol. 16:955-966(1991).
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_00860}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00860}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_00860}.
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_00860}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00860}.
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DR   EMBL; X55937; CAA39402.1; -; Genomic_DNA.
DR   PIR; S16253; RKRPF1.
DR   RefSeq; XP_013725634.1; XM_013870180.1.
DR   RefSeq; XP_013741773.1; XM_013886319.1.
DR   AlphaFoldDB; P27985; -.
DR   SMR; P27985; -.
DR   EnsemblPlants; CDY71122; CDY71122; GSBRNA2T00011400001.
DR   GeneID; 106429432; -.
DR   GeneID; 106444895; -.
DR   Gramene; CDY71122; CDY71122; GSBRNA2T00011400001.
DR   KEGG; bna:106429432; -.
DR   KEGG; bna:106444895; -.
DR   OMA; RKNWVPC; -.
DR   GO; GO:0009507; C:chloroplast; 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; IPR024680; RuBisCO_ssu_N.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR31262; PTHR31262; 1.
DR   Pfam; PF12338; RbcS; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   PRINTS; PR00152; RUBISCOSMALL.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; SSF55239; 1.
PE   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Chloroplast; Photorespiration;
KW   Photosynthesis; Plastid; Transit peptide.
FT   TRANSIT         1..54
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT   CHAIN           55..181
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   chloroplastic 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031470"
SQ   SEQUENCE   181 AA;  20183 MW;  0B082641A8D5815C CRC64;
     MASSMLSSAA VVTSPAQATM VAPFTGLKSS AAFPVTRKAN NDITSIASNG GRVSCMKVWP
     PVGKKKFETL SYLPDLTEVE LGKEVDYLLR NKWIPCVEFE LEHGFVYREH GSTPGYYDGR
     YWTMWKLPLF GCTDSAQVLK EVQECKTEYP NAFIRIIGFD NNRQVQCISF IAYKPPSFTG
     A