ID   RBS1_HYDCU              Reviewed;         116 AA.
AC   Q31IJ9;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00859};
DE            Short=RuBisCO small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00859};
DE   AltName: Full=Non-carboxysomal form I RuBisCO small subunit {ECO:0000303|PubMed:28115547};
GN   Name=cbbS1 {ECO:0000255|HAMAP-Rule:MF_00859}; OrderedLocusNames=Tcr_0428;
OS   Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS   crunogena).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Hydrogenovibrio.
OX   NCBI_TaxID=317025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25203 / XCL-2;
RX   PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA   Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA   Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA   Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA   Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA   Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA   Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA   Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA   Tinkham L.E., Zeruth G.T.;
RT   "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT   XCL-2.";
RL   PLoS Biol. 4:1-17(2006).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=DSM 25203 / XCL-2;
RX   PubMed=18974784; DOI=10.1371/journal.pone.0003570;
RA   Menon B.B., Dou Z., Heinhorst S., Shively J.M., Cannon G.C.;
RT   "Halothiobacillus neapolitanus carboxysomes sequester heterologous and
RT   chimeric RubisCO species.";
RL   PLoS ONE 3:e3570-e3570(2008).
RN   [3]
RP   INDUCTION.
RC   STRAIN=DSM 25203 / XCL-2;
RX   PubMed=28115547; DOI=10.1128/jb.00871-16;
RG   USF MCB4404L;
RA   Mangiapia M., Brown T.W., Chaput D., Haller E., Harmer T.L., Hashemy Z.,
RA   Keeley R., Leonard J., Mancera P., Nicholson D., Stevens S., Wanjugi P.,
RA   Zabinski T., Pan C., Scott K.M.;
RT   "Proteomic and Mutant Analysis of the CO2 Concentrating Mechanism of
RT   Hydrothermal Vent Chemolithoautotroph Thiomicrospira crunogena.";
RL   J. Bacteriol. 199:0-0(2017).
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:0000305|PubMed:18974784}.
CC   -!- FUNCTION: Can replace the endogenous type I ccbS gene in
CC       H.neapolitanus, reconstituting RuBisCO with about 10% of normal
CC       activity; the active enzyme is targeted to carboxysomes
CC       (PubMed:18974784). {ECO:0000269|PubMed:18974784}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00859}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:18974784}.
CC   -!- INDUCTION: Induced by growth in high levels of dissolved inorganic
CC       carbon and low NH(3) levels (at protein level).
CC       {ECO:0000269|PubMed:28115547}.
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}.
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DR   EMBL; CP000109; ABB41024.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q31IJ9; -.
DR   SMR; Q31IJ9; -.
DR   STRING; 317025.Tcr_0428; -.
DR   EnsemblBacteria; ABB41024; ABB41024; Tcr_0428.
DR   KEGG; tcx:Tcr_0428; -.
DR   eggNOG; COG4451; Bacteria.
DR   HOGENOM; CLU_098114_2_0_6; -.
DR   OMA; WNPAIEH; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd03527; RuBisCO_small; 1.
DR   Gene3D; 3.30.190.10; -; 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; PTHR31262; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; SSF55239; 1.
PE   1: Evidence at protein level;
KW   Calvin cycle; Carbon dioxide fixation; Cytoplasm.
FT   CHAIN           1..116
FT                   /note="Ribulose bisphosphate carboxylase small subunit 1"
FT                   /id="PRO_0000452046"
SQ   SEQUENCE   116 AA;  13343 MW;  9B7D40E650E5F98C CRC64;
     MSIQDYPSRL SDPQSRKAET FSYLPKMTAE QIKAQVQYII DRGWNPAIEH SEPENAFSYY
     WYMWKLPMFG ETDADAVLAE VDACIKANPN NHVRLIGYDN YAQSQGANML VKRGDM