ID   RBS1_SOLTU              Reviewed;         181 AA.
AC   P10647;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 1 {ECO:0000255|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00860};
DE   AltName: Full=Ribulose bisphosphate carboxylase small chain C, chloroplastic;
DE            Short=RuBisCO small subunit C;
DE   Flags: Precursor;
GN   Name=RBCS1 {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS-C;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. HH1201/7;
RX   PubMed=3422467; DOI=10.1073/pnas.85.3.846;
RA   Wolter F.P., Fritz C.C., Willmitzer L., Schell J., Schreier P.H.;
RT   "rbcS genes in Solanum tuberosum: conservation of transit peptide and exon
RT   shuffling during evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:846-850(1988).
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; J03613; AAA33838.1; -; mRNA.
DR   PIR; A31083; RKPOSC.
DR   RefSeq; NP_001275244.1; NM_001288315.1.
DR   AlphaFoldDB; P10647; -.
DR   SMR; P10647; -.
DR   STRING; 4113.PGSC0003DMT400062138; -.
DR   PRIDE; P10647; -.
DR   GeneID; 102605737; -.
DR   KEGG; sot:102605737; -.
DR   eggNOG; ENOG502QT0M; Eukaryota.
DR   InParanoid; P10647; -.
DR   OrthoDB; 1258997at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P10647; baseline and differential.
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   2: Evidence at transcript level;
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 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031550"
SQ   SEQUENCE   181 AA;  20368 MW;  033A8785B8A42AB0 CRC64;
     MASSIVSSAA VATRSNVAQA SMVAPFTGLK SAASFPVTKK NNNVDITSLA SNGGRVRCMQ
     VWPPINMKKY ETLSYLPDLS DEQLLKEVEY LLKNGWVPCL EFETEHGFVY REHNSSPGYY
     DGRYWTMWKL PMFGCTDGTQ VLAEVQEAKN AYPQAWIRII GFDNVRQVQC ISFIAYKPEG
     Y