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Database: UniProt
Entry: RBS2_NICSY
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Original site: RBS2_NICSY 
ID   RBS2_NICSY              Reviewed;         181 AA.
AC   P22433;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   27-MAR-2024, entry version 102.
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};
OS   Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4096;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2388836; DOI=10.1093/nar/18.15.4589;
RA   Jamet E., Fargeas C., Durr A., Fleck J.;
RT   "Nucleotide sequences of two genes encoding the small subunit of RUBISCO in
RT   Nicotiana sylvestris.";
RL   Nucleic Acids Res. 18:4589-4589(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_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; X53426; CAA37516.1; -; Genomic_DNA.
DR   PIR; S10987; RKNT41.
DR   RefSeq; XP_009758143.1; XM_009759841.1.
DR   AlphaFoldDB; P22433; -.
DR   SMR; P22433; -.
DR   STRING; 4096.P22433; -.
DR   GeneID; 104210868; -.
DR   KEGG; nsy:104210868; -.
DR   eggNOG; ENOG502QT0M; Eukaryota.
DR   OrthoDB; 5482775at2759; -.
DR   Proteomes; UP000189701; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
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; IPR024680; RuBisCO_ssu_N.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31262:SF10; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT, CHLOROPLASTIC 2; 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; RuBisCO, small subunit; 1.
PE   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Chloroplast; Photorespiration;
KW   Photosynthesis; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT   CHAIN           58..181
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   chloroplastic 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031536"
SQ   SEQUENCE   181 AA;  20474 MW;  4925591654E8D81B CRC64;
     MAFLIMSSAA AVATGTNAAQ ASMIAPFTGL KSATSFPVSR KQNLDITSIA SNGGRVQCMQ
     VWPPINKKKY ETLSYLPDLS EEQLLREVEY LLKNGWVPCL EFETEHGFVY RENNKSPGYY
     DGRYWTMWKL PMFGCTDATQ VLAEVEEAKK AYPQAWIRII GFDNVRQVQC ISFIAYKPEG
     Y
//
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