ID   A9BEH4_PROM4            Unreviewed;       113 AA.
AC   A9BEH4;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000256|HAMAP-Rule:MF_00859};
DE            Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00859};
GN   Name=rbcS {ECO:0000256|HAMAP-Rule:MF_00859,
GN   ECO:0000313|EMBL:ABX08484.1};
GN   Synonyms=cbbS {ECO:0000256|HAMAP-Rule:MF_00859};
GN   OrderedLocusNames=P9211_05531 {ECO:0000313|EMBL:ABX08484.1};
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=93059 {ECO:0000313|EMBL:ABX08484.1, ECO:0000313|Proteomes:UP000000788};
RN   [1] {ECO:0000313|EMBL:ABX08484.1, ECO:0000313|Proteomes:UP000000788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211 {ECO:0000313|Proteomes:UP000000788};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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 in the photorespiration process. Both reactions occur
CC       simultaneously and in competition at the same active site. Although the
CC       small subunit is not catalytic it is essential for maximal activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00859}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00859}.
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000256|HAMAP-Rule:MF_00859}.
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_00859}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_00859}.
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DR   EMBL; CP000878; ABX08484.1; -; Genomic_DNA.
DR   RefSeq; WP_012195106.1; NC_009976.1.
DR   AlphaFoldDB; A9BEH4; -.
DR   STRING; 93059.P9211_05531; -.
DR   KEGG; pmj:P9211_05531; -.
DR   eggNOG; COG4451; Bacteria.
DR   HOGENOM; CLU_098114_2_0_3; -.
DR   OrthoDB; 9788955at2; -.
DR   Proteomes; UP000000788; Chromosome.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
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   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; RuBisCO, small subunit; 1.
PE   3: Inferred from homology;
KW   Bacterial microcompartment {ECO:0000256|HAMAP-Rule:MF_00859};
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP-
KW   Rule:MF_00859};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00859}; Carboxysome {ECO:0000256|HAMAP-Rule:MF_00859};
KW   Lyase {ECO:0000313|EMBL:ABX08484.1};
KW   Photorespiration {ECO:0000256|HAMAP-Rule:MF_00859};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00859};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000788}.
FT   DOMAIN          15..112
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   113 AA;  12991 MW;  C8FA514FBA72A36A CRC64;
     MPFQSTVGDY QTVATLETFG FLPPMTQDEI YDQIAYIIAQ GWSPVIEHVH PSGSMQTYWS
     YWKLPFFGEK DLNVVVSELE ACHRAYPDHH VRMVGYDAYT QSQGTCFVVF EGR
//