ID   RBS_LARLA               Reviewed;         189 AA.
AC   P16031;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00860};
DE   Flags: Precursor;
GN   Name=RBCS {ECO:0000255|HAMAP-Rule:MF_00860};
OS   Larix laricina (Tamarack) (Pinus laricina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Larix.
OX   NCBI_TaxID=3326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Needle;
RX   PubMed=2101694; DOI=10.1007/bf00018569;
RA   Hutchison K.W., Harvie P.D., Singer P.B., Brunner A.F., Greenwood M.G.;
RT   "Nucleotide sequence of the small subunit of ribulose-1,5-bisphosphate
RT   carboxylase from the conifer Larix laricina.";
RL   Plant Mol. Biol. 14:281-284(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; X16039; CAA34161.1; -; Genomic_DNA.
DR   PIR; S15771; RKKHS.
DR   AlphaFoldDB; P16031; -.
DR   SMR; P16031; -.
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; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR31262; PTHR31262; 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..66
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT   CHAIN           67..189
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   chloroplastic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031511"
SQ   SEQUENCE   189 AA;  21191 MW;  B546BF7AAE87DB77 CRC64;
     MASSIMALSS TAAVAAVAAP SKTGNSNVVS AFTGLKSMAQ FPSSKTMSNA GAEWEQKTTS
     NGSRVRCMQV WPPYANKKFE TLSYLPRLTP EQLVKEVEYL LKNKWVPCLE FEEDGEIKRV
     YGNSPGYYDG RYWVMWKLPM FGCTEASQVL NEVNECAKAY PNAFIRVIGF DNVRQVQCIS
     FIVHKPEYN