ID   F8C112_AFIC5            Unreviewed;       141 AA.
AC   F8C112;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
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:AEI08122.1};
GN   OrderedLocusNames=OCA5_pHCG300480 {ECO:0000313|EMBL:AEI08122.1};
OS   Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS   (Oligotropha carboxidovorans).
OG   Plasmid pHCG3 {ECO:0000313|EMBL:AEI08122.1,
OG   ECO:0000313|Proteomes:UP000007730}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=504832 {ECO:0000313|EMBL:AEI08122.1, ECO:0000313|Proteomes:UP000007730};
RN   [1] {ECO:0000313|EMBL:AEI08122.1, ECO:0000313|Proteomes:UP000007730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5
RC   {ECO:0000313|Proteomes:UP000007730};
RC   PLASMID=pHCG3 {ECO:0000313|EMBL:AEI08122.1};
RX   PubMed=14644498; DOI=10.1016/j.gene.2003.08.027;
RA   Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.;
RT   "Complete nucleotide sequence of the circular megaplasmid pHCG3 of
RT   Oligotropha carboxidovorans: function in the chemolithoautotrophic
RT   utilization of CO, H(2) and CO(2).";
RL   Gene 322:67-75(2003).
RN   [2] {ECO:0000313|EMBL:AEI08122.1, ECO:0000313|Proteomes:UP000007730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5
RC   {ECO:0000313|Proteomes:UP000007730};
RC   PLASMID=pHCG3 {ECO:0000313|EMBL:AEI08122.1};
RX   PubMed=21742883; DOI=10.1128/JB.05619-11;
RA   Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA   Meyer O.;
RT   "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT   carboxidovorans strains OM4 and OM5.";
RL   J. Bacteriol. 193:5043-5043(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}.
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DR   EMBL; CP002827; AEI08122.1; -; Genomic_DNA.
DR   RefSeq; WP_013913746.1; NC_015689.1.
DR   AlphaFoldDB; F8C112; -.
DR   KEGG; ocg:OCA5_pHCG300480; -.
DR   PATRIC; fig|504832.7.peg.3623; -.
DR   HOGENOM; CLU_098114_2_0_5; -.
DR   OrthoDB; 9788955at2; -.
DR   Proteomes; UP000007730; Plasmid pHCG3.
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:AEI08122.1};
KW   Plasmid {ECO:0000313|EMBL:AEI08122.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007730}.
FT   DOMAIN          4..103
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   141 AA;  16555 MW;  DF27B4795FE209D3 CRC64;
     MRITQGCFSF LPDLTDEQIK KQIQYCLGKD WAVNIEFTDD PHPRNTYWEM WGLPMFDLRD
     AAGIMMELKE CRKVYGDRYI RINAFDSSHG WESVRISFIV NRPKNEPGFR LARQEVGGRN
     MRYTTTSYAA DRPEGQRYNG A
//