ID   A1WVV9_HALHL            Unreviewed;       119 AA.
AC   A1WVV9;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
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   OrderedLocusNames=Hhal_1045 {ECO:0000313|EMBL:ABM61821.1};
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124 {ECO:0000313|EMBL:ABM61821.1, ECO:0000313|Proteomes:UP000000647};
RN   [1] {ECO:0000313|Proteomes:UP000000647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA   Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABM61821.1, ECO:0000313|Proteomes:UP000000647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RX   PubMed=23991253; DOI=10.4056/sigs.3677284;
RA   Challacombe J.F., Majid S., Deole R., Brettin T.S., Bruce D., Delano S.F.,
RA   Detter J.C., Gleasner C.D., Han C.S., Misra M., Reitenga K.G.,
RA   Mikhailova N., Woyke T., Pitluck S., Nolan M., Land M.L., Saunders E.,
RA   Tapia R., Lapidus A., Ivanova N., Hoff W.D.;
RT   "Complete genome sequence of Halorhodospira halophila SL1.";
RL   Stand. Genomic Sci. 8:206-214(2013).
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|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; CP000544; ABM61821.1; -; Genomic_DNA.
DR   RefSeq; WP_011813844.1; NC_008789.1.
DR   AlphaFoldDB; A1WVV9; -.
DR   STRING; 349124.Hhal_1045; -.
DR   KEGG; hha:Hhal_1045; -.
DR   eggNOG; COG4451; Bacteria.
DR   HOGENOM; CLU_098114_2_0_6; -.
DR   OrthoDB; 9788955at2; -.
DR   Proteomes; UP000000647; 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   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:ABM61821.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000647}.
FT   DOMAIN          18..115
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   119 AA;  13998 MW;  AE92F3D01AA3733F CRC64;
     MSEIQDYNSK LSDPNSRRFE TFSYLPEMSD ADVRKQVQYI VDQGWNPAIE HTEPENAFDH
     YWYMWKLPMF GETDVDAILK EAEACHKAHP EHHVRLIGYD NYRQTQGTAM VIYRGPIDA
//