RBS_SYNY3
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 03-AUG-2022, entry version 128.
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}; OrderedLocusNames=slr0012;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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; 1148.1001565; -.
DR PaxDb; P54206; -.
DR EnsemblBacteria; BAA10192; BAA10192; BAA10192.
DR KEGG; syn:slr0012; -.
DR eggNOG; COG4451; Bacteria.
DR InParanoid; P54206; -.
DR OMA; KQCQVLS; -.
DR PhylomeDB; P54206; -.
DR BioCyc; MetaCyc:MON-751; -.
DR SABIO-RK; P54206; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
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 SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; SSF55239; 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
