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Database: UniProt
Entry: H0TXL1_9BRAD
LinkDB: H0TXL1_9BRAD
Original site: H0TXL1_9BRAD 
ID   H0TXL1_9BRAD            Unreviewed;       140 AA.
AC   H0TXL1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   ECO:0000313|EMBL:CCE11199.1};
GN   ORFNames=BRAS3843_660007 {ECO:0000313|EMBL:CCE11199.1};
OS   Bradyrhizobium sp. STM 3843.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE11199.1, ECO:0000313|Proteomes:UP000002686};
RN   [1] {ECO:0000313|Proteomes:UP000002686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(2011).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCE11199.1}.
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DR   EMBL; CAFK01000314; CCE11199.1; -; Genomic_DNA.
DR   RefSeq; WP_008973707.1; NZ_CAFK01000314.1.
DR   AlphaFoldDB; H0TXL1; -.
DR   OrthoDB; 9788955at2; -.
DR   Proteomes; UP000002686; Unassembled WGS sequence.
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}; Lyase {ECO:0000313|EMBL:CCE11199.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002686}.
FT   DOMAIN          4..103
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   140 AA;  16443 MW;  B656EE305298C049 CRC64;
     MRVTQGCFSF LPDLTDEQIT AQVQYCLDKG WAVNIEFTDD PHPRNTYWEM WGLPMFDLRD
     AAGIMRELAD CRKIYGDRYI RISGFDSSHG WESLRISFIV NRPQHEPGFR LDRQETVGRN
     LRYATHAYAT ERPEGERYSS
//
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