ID   RBS_SYNY3               Reviewed;         113 AA.
AC   P54206;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000255|HAMAP-Rule:MF_00859};
DE            Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00859};
GN   Name=cbbS {ECO:0000255|HAMAP-Rule:MF_00859};
GN   Synonyms=rbcS {ECO:0000255|HAMAP-Rule:MF_00859};
GN   OrderedLocusNames=slr0012;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8219082; DOI=10.1007/bf00019295;
RA   Amichay D., Levitz R., Gurevitz M.;
RT   "Construction of a Synechocystis PCC6803 mutant suitable for the study of
RT   variant hexadecameric ribulose bisphosphate carboxylase/oxygenase
RT   enzymes.";
RL   Plant Mol. Biol. 23:465-476(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-11.
RX   PubMed=9298645; DOI=10.1002/elps.1150180806;
RA   Sazuka T., Ohara O.;
RT   "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT   PCC6803: linking 130 protein spots with their respective genes.";
RL   Electrophoresis 18:1252-1258(1997).
RN   [5]
RP   INTERACTION WITH CCMM, AND SUBCELLULAR LOCATION.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=17993516; DOI=10.1128/jb.01283-07;
RA   Cot S.S., So A.K., Espie G.S.;
RT   "A multiprotein bicarbonate dehydration complex essential to carboxysome
RT   function in cyanobacteria.";
RL   J. Bacteriol. 190:936-945(2008).
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:0000255|HAMAP-Rule:MF_00859}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits. RuBisCO
CC       interacts with the C-terminus of CcmM, and can be found in complexes
CC       that also include carbonic anhydrase (ccaA) (PubMed:17993516).
CC       {ECO:0000269|PubMed:17993516}.
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00859,
CC       ECO:0000269|PubMed:17993516}. Note=This cyanobacterium makes beta-type
CC       carboxysomes. RuBisCO associates with both the internal and shell
CC       portion of carboxysomes (PubMed:17993516). In the carboxysome RuBisCO
CC       is organized into a paracrystalline array (By similarity).
CC       {ECO:0000250|UniProtKB:Q31NB2, ECO:0000269|PubMed:17993516}.
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_00859}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00859}.
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DR   EMBL; X65960; CAA46774.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA10192.1; -; Genomic_DNA.
DR   PIR; S39562; S39562.
DR   AlphaFoldDB; P54206; -.
DR   SMR; P54206; -.
DR   IntAct; P54206; 17.
DR   STRING; 1148.gene:10499689; -.
DR   PaxDb; 1148-1001565; -.
DR   EnsemblBacteria; BAA10192; BAA10192; BAA10192.
DR   KEGG; syn:slr0012; -.
DR   eggNOG; COG4451; Bacteria.
DR   InParanoid; P54206; -.
DR   PhylomeDB; P54206; -.
DR   BioCyc; MetaCyc:MONOMER-751; -.
DR   SABIO-RK; P54206; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Bacterial microcompartment; Calvin cycle; Carbon dioxide fixation;
KW   Carboxysome; Direct protein sequencing; Photorespiration; Photosynthesis;
KW   Reference proteome.
FT   CHAIN           1..113
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /id="PRO_0000198627"
SQ   SEQUENCE   113 AA;  13239 MW;  20C762A777F4E623 CRC64;
     MKTLPKERRY ETLSYLPPLT DQQIAKQVEF LLDQGFIPGV EFEEDPQPET HFWTMWKLPF
     FGGATANEVL AEVRECRSEN PNCYIRVIGF DNIKQCQTVS FIVHKPNQNQ GRY
//