ID   K0DSS8_9BURK            Unreviewed;       142 AA.
AC   K0DSS8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=cbbS {ECO:0000256|HAMAP-Rule:MF_00859};
GN   ORFNames=BUPH_00546 {ECO:0000313|EMBL:AFT88010.1};
OS   Paraburkholderia phenoliruptrix BR3459a.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1229205 {ECO:0000313|EMBL:AFT88010.1, ECO:0000313|Proteomes:UP000010105};
RN   [1] {ECO:0000313|EMBL:AFT88010.1, ECO:0000313|Proteomes:UP000010105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR3459a {ECO:0000313|EMBL:AFT88010.1,
RC   ECO:0000313|Proteomes:UP000010105};
RX   PubMed=23144415; DOI=10.1128/JB.01821-12;
RA   de Oliveira Cunha C., Goda Zuleta L.F., Paula de Almeida L.G.,
RA   Prioli Ciapina L., Lustrino Borges W., Pitard R.M., Baldani J.I.,
RA   Straliotto R., de Faria S.M., Hungria M., Sousa Cavada B., Mercante F.M.,
RA   Ribeiro de Vasconcelos A.T.;
RT   "Complete Genome Sequence of Burkholderia phenoliruptrix BR3459a (CLA1), a
RT   Heat-Tolerant, Nitrogen-Fixing Symbiont of Mimosa flocculosa.";
RL   J. Bacteriol. 194:6675-6676(2012).
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_00859}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000256|ARBA:ARBA00038826, 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; CP003864; AFT88010.1; -; Genomic_DNA.
DR   RefSeq; WP_014972037.1; NC_018672.1.
DR   AlphaFoldDB; K0DSS8; -.
DR   STRING; 1229205.BUPH_00546; -.
DR   GeneID; 27799280; -.
DR   KEGG; bpx:BUPH_00546; -.
DR   PATRIC; fig|1229205.11.peg.4412; -.
DR   eggNOG; COG4451; Bacteria.
DR   HOGENOM; CLU_098114_2_0_4; -.
DR   Proteomes; UP000010105; Chromosome 2.
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   PANTHER; PTHR31262:SF23; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT; 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   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}.
FT   DOMAIN          4..103
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
FT   REGION          123..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   142 AA;  16308 MW;  B3EF0F0C04AC7438 CRC64;
     MRITQGTFSF LPELTDEEIS LQIDYALSQG WACSVEFTDD PHPRNTYWEM WGLPMFDLHD
     AAGVLQEVKA CRAARPDHYI KINAFDSVRG FETMRLSFIV NRPEEEPGFR LTREDGPGRV
     QRYGLAGYAS ERPAGQRYGT ER
//