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Database: UniProt
Entry: A0A2G2XBI7_CAPBA
LinkDB: A0A2G2XBI7_CAPBA
Original site: A0A2G2XBI7_CAPBA 
ID   A0A2G2XBI7_CAPBA        Unreviewed;       180 AA.
AC   A0A2G2XBI7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00860};
GN   Name=RBCS {ECO:0000256|HAMAP-Rule:MF_00860};
GN   ORFNames=CQW23_03331 {ECO:0000313|EMBL:PHT54845.1};
OS   Capsicum baccatum (Peruvian pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=33114 {ECO:0000313|EMBL:PHT54845.1, ECO:0000313|Proteomes:UP000224567};
RN   [1] {ECO:0000313|EMBL:PHT54845.1, ECO:0000313|Proteomes:UP000224567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PHT54845.1};
RX   PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA   Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA   Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA   Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA   Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA   Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA   Bennetzen J.L., Choi D.;
RT   "New reference genome sequences of hot pepper reveal the massive evolution
RT   of plant disease-resistance genes by retroduplication.";
RL   Genome Biol. 18:R210.1-R210.11(2017).
RN   [2] {ECO:0000313|Proteomes:UP000224567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RA   Kim S., Park J., Yeom S.-I., Kim Y.-M., Seo E., Kim K.-T., Kim M.-S.,
RA   Lee J.M., Cheong K., Shin H.-S., Kim S.-B., Han K., Lee J., Park M.,
RA   Lee H.-A., Lee H.-Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E.,
RA   Jeon J., Kim H., Choi G., Song H., Lee J., Lee S.-C., Kwon J.-K.,
RA   Lee H.-Y., Koo N., Hong Y., Kim R.W., Kang W.-H., Huh J.H., Kang B.-C.,
RA   Yang T.-J., Lee Y.-H., Bennetzen J.L., Choi D.;
RT   "Multiple reference genome sequences of hot pepper reveal the massive
RT   evolution of plant disease resistance genes by retroduplication.";
RL   J. Anim. Genet. bioRxivorg:115410-115410(2017).
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:0000256|HAMAP-Rule:MF_00860,
CC       ECO:0000256|RuleBase:RU003627}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, plasmodesma
CC       {ECO:0000256|ARBA:ARBA00024184}. Plastid, chloroplast
CC       {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_00860}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHT54845.1}.
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DR   EMBL; MLFT02000002; PHT54845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G2XBI7; -.
DR   STRING; 33114.A0A2G2XBI7; -.
DR   Proteomes; UP000224567; Chromosome 2.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-SubCell.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP-
KW   Rule:MF_00860};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00860}; Chloroplast {ECO:0000256|HAMAP-Rule:MF_00860};
KW   Photorespiration {ECO:0000256|ARBA:ARBA00023238, ECO:0000256|HAMAP-
KW   Rule:MF_00860};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_00860};
KW   Plastid {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224567};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          68..177
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   180 AA;  20443 MW;  77D2EFD00BC24989 CRC64;
     MASSVISSAA VATRTNVTQA SMVAPFTGLK SAASFPVTRK NNLDITSIAS NGGRVQCMLV
     WPPINKKKYE TLSYLPDLSD EQLLKEIEYL LQKGWVPCLE FETEHGFVYR EHHKSPGYYD
     GRYWTMWKLP MFGCTDATQV LNEVQEAKKA YPQAWVRIIG FDNVRQVQCI SFIAYKPEGY
//
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