ID   RBS2_ALLVD              Reviewed;         113 AA.
AC   P22860; D3RQ47;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit 2 {ECO:0000255|HAMAP-Rule:MF_00859};
DE            Short=RuBisCO small subunit 2 {ECO:0000255|HAMAP-Rule:MF_00859};
GN   Name=cbbS2 {ECO:0000255|HAMAP-Rule:MF_00859};
GN   Synonyms=rbcS {ECO:0000303|PubMed:1899846};
GN   OrderedLocusNames=Alvin_2749;
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS   10441 / D) (Chromatium vinosum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=572477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND SUBUNIT.
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=1899846; DOI=10.1016/0378-1119(91)90009-z;
RA   Kobayashi H., Viale A.M., Takabe T., Akazawa T., Wada K., Shinozaki K.,
RA   Kobayashi K., Sugiura M.;
RT   "Sequence and expression of genes encoding the large and small subunits of
RT   ribulose 1,5-bisphosphate carboxylase/oxygenase from Chromatium vinosum.";
RL   Gene 97:55-62(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-24, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RX   PubMed=2211708; DOI=10.1016/s0021-9258(17)44764-8;
RA   Viale A.M., Kobayashi H., Akazawa T.;
RT   "Distinct properties of Escherichia coli products of plant-type
RT   ribulose-1,5-bisphosphate carboxylase/oxygenase directed by two sets of
RT   genes from the photosynthetic bacterium Chromatium vinosum.";
RL   J. Biol. Chem. 265:18386-18392(1990).
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:0000255|HAMAP-Rule:MF_00859,
CC       ECO:0000269|PubMed:1899846, ECO:0000269|PubMed:2211708}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=32.8 uM for CO2 purified from A.vinosum in vivo
CC         {ECO:0000269|PubMed:2211708};
CC         KM=71.6 uM for CO2, enzyme expressed in E.coli
CC         {ECO:0000269|PubMed:1899846, ECO:0000269|PubMed:2211708};
CC         KM=14.2 uM for D-ribulose 1,5-bisphosphate purified from A.vinosum in
CC         vivo {ECO:0000269|PubMed:2211708};
CC         KM=22.1 uM for D-ribulose 1,5-bisphosphate, enzyme expressed in
CC         E.coli {ECO:0000269|PubMed:2211708};
CC         Vmax=6.2 umol/min/mg enzyme purified from A.vinosum in vivo
CC         {ECO:0000269|PubMed:1899846, ECO:0000269|PubMed:2211708};
CC         Vmax=5.9 umol/min/mg enzyme expressed in E.coli
CC         {ECO:0000269|PubMed:2211708};
CC         Note=This enzyme requires a lac or tac promoter for expression in
CC         E.coli and has different kinetics than the enzyme purified in vivo,
CC         suggesting this is not expressed in A.vinosum.
CC         {ECO:0000269|PubMed:1899846, ECO:0000269|PubMed:2211708};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|PubMed:2211708}.
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}.
CC   -!- CAUTION: In C.vinosum two similar set of genes code for RuBisCO large
CC       and small chains: the RbcL-RbcS (this entry) and the RbcA-RbcB pair.
CC       Under standard photoautotrophic culture conditions only the latter pair
CC       seems active, the former being probably cryptic.
CC       {ECO:0000269|PubMed:1899846, ECO:0000269|PubMed:2211708}.
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DR   EMBL; D90204; BAA14230.1; -; Genomic_DNA.
DR   EMBL; CP001896; ADC63658.1; -; Genomic_DNA.
DR   PIR; JQ0587; RKKRS2.
DR   RefSeq; WP_012971926.1; NC_013851.1.
DR   AlphaFoldDB; P22860; -.
DR   SMR; P22860; -.
DR   STRING; 572477.Alvin_2749; -.
DR   KEGG; alv:Alvin_2749; -.
DR   eggNOG; COG4451; Bacteria.
DR   HOGENOM; CLU_098114_2_0_6; -.
DR   OrthoDB; 9788955at2; -.
DR   Proteomes; UP000001441; Chromosome.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; 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   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; RuBisCO, small subunit; 1.
PE   1: Evidence at protein level;
KW   Calvin cycle; Carbon dioxide fixation; Direct protein sequencing;
KW   Photosynthesis; Reference proteome.
FT   CHAIN           1..113
FT                   /note="Ribulose bisphosphate carboxylase small subunit 2"
FT                   /id="PRO_0000198613"
FT   CONFLICT        109
FT                   /note="V -> A (in Ref. 1; BAA14230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="A -> P (in Ref. 1; BAA14230)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   113 AA;  13393 MW;  00376BC870FF3399 CRC64;
     MNTASSMGDH ATIGRYETFS YLPPLNREEI LEQILYILDN GWNASLEHEH PDRAFEYYWP
     MWKMPFFGEQ DPNVILTEIE SCRRSYPDHH VRLVGYDTYA QSKGHSFLVH RAR
//