ID   RBS_BATOE               Reviewed;         175 AA.
AC   P26985;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 91.
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   Batophora oerstedii (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC   Dasycladales; Dasycladaceae; Batophora.
OX   NCBI_TaxID=3140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1934113; DOI=10.1007/bf00312782;
RA   Schneider S.U., de Groot E.J.;
RT   "Sequences of two rbcS cDNA clones of Batophora oerstedii: structural and
RT   evolutionary considerations.";
RL   Curr. Genet. 20:173-175(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; X57266; CAA40538.1; -; mRNA.
DR   PIR; S18022; S18022.
DR   AlphaFoldDB; P26985; -.
DR   SMR; P26985; -.
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   2: Evidence at transcript level;
KW   Calvin cycle; Carbon dioxide fixation; Chloroplast; Photorespiration;
KW   Photosynthesis; Plastid; Transit peptide.
FT   TRANSIT         1..34
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT   CHAIN           35..175
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   chloroplastic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031467"
SQ   SEQUENCE   175 AA;  20110 MW;  D9F833269E4A2022 CRC64;
     MSFATTNKTI VPCATTKQIV RPRFLSNGTI SKSRAMMVWE PFNNKFFETF SYLPPLTDDQ
     ITKQVDYILR NNWTPCLEFA GSDQAYVTHD NTVRMGDCAS TYQDNRYWTM WKLPMFGCID
     GSQVLTEISA CTKAFPDAYI RLVCFDANRQ VQISGFLVHR PESATDYRLP ADRQV