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Database: UniProt/TrEMBL
Entry: A4SA23_OSTLU
LinkDB: A4SA23_OSTLU
Original site: A4SA23_OSTLU 
ID   A4SA23_OSTLU            Unreviewed;       177 AA.
AC   A4SA23;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   03-MAY-2023, entry version 84.
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=OSTLU_89572 {ECO:0000313|EMBL:ABP00483.1};
OS   Ostreococcus lucimarinus (strain CCE9901).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=436017 {ECO:0000313|EMBL:ABP00483.1, ECO:0000313|Proteomes:UP000001568};
RN   [1] {ECO:0000313|EMBL:ABP00483.1, ECO:0000313|Proteomes:UP000001568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCE9901 {ECO:0000313|EMBL:ABP00483.1,
RC   ECO:0000313|Proteomes:UP000001568};
RX   PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA   Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA   Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA   Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA   Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA   Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA   Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA   Van de Peer Y., Moreau H., Grigoriev I.V.;
RT   "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT   of plankton speciation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
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: Plastid, chloroplast {ECO:0000256|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: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}.
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DR   EMBL; CP000597; ABP00483.1; -; Genomic_DNA.
DR   RefSeq; XP_001422166.1; XM_001422129.1.
DR   AlphaFoldDB; A4SA23; -.
DR   STRING; 436017.A4SA23; -.
DR   EnsemblPlants; ABP00483; ABP00483; OSTLU_89572.
DR   GeneID; 5006224; -.
DR   Gramene; ABP00483; ABP00483; OSTLU_89572.
DR   KEGG; olu:OSTLU_89572; -.
DR   eggNOG; ENOG502QT0M; Eukaryota.
DR   HOGENOM; CLU_098114_2_0_1; -.
DR   OMA; HAFVYRE; -.
DR   OrthoDB; 5482775at2759; -.
DR   Proteomes; UP000001568; Chromosome 17.
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-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; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 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:UP000001568}.
FT   DOMAIN          46..162
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   177 AA;  20119 MW;  B558D319F5B22CFC CRC64;
     MLGAGGCFVL GSDAVHERRH GWASVEDSRE RCTDRFRFVF TSSRRMFETF SFLPPLSDAE
     ISKQVQYLLN NGWTPCIEFE DSAHAYTDGH GWANMDTSIN AGYYDNRYWV MWKLPMYGCQ
     NPDEVIAEIN TCIKCFPDCY VRVAGFDNIK QVQCSAFLAH RPASEAACAV DQRQVQG
//
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