ID   F0IX25_ACIMA            Unreviewed;       142 AA.
AC   F0IX25;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
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:BAJ80435.1};
GN   OrderedLocusNames=ACMV_10880 {ECO:0000313|EMBL:BAJ80435.1};
GN   ORFNames=Apmu_0115_08 {ECO:0000313|EMBL:GAN73793.1};
OS   Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / AIU
OS   301).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=926570 {ECO:0000313|EMBL:BAJ80435.1, ECO:0000313|Proteomes:UP000007100};
RN   [1] {ECO:0000313|EMBL:BAJ80435.1, ECO:0000313|Proteomes:UP000007100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AIU301 {ECO:0000313|EMBL:BAJ80435.1}, and DSM 11245 / JCM 8867
RC   / AIU301 {ECO:0000313|Proteomes:UP000007100};
RA   Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H.,
RA   Hosoyama A., Yamada R., Fujita N.;
RT   "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAN73793.1, ECO:0000313|Proteomes:UP000032662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AIU301 {ECO:0000313|EMBL:GAN73793.1,
RC   ECO:0000313|Proteomes:UP000032662};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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; AP012035; BAJ80435.1; -; Genomic_DNA.
DR   EMBL; BANA01000113; GAN73793.1; -; Genomic_DNA.
DR   RefSeq; WP_007422834.1; NZ_BANA01000113.1.
DR   AlphaFoldDB; F0IX25; -.
DR   KEGG; amv:ACMV_10880; -.
DR   HOGENOM; CLU_098114_2_0_5; -.
DR   OrthoDB; 9788955at2; -.
DR   Proteomes; UP000007100; Chromosome.
DR   Proteomes; UP000032662; 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:BAJ80435.1}.
FT   DOMAIN          4..103
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   142 AA;  16617 MW;  92C18CDB3CEB2990 CRC64;
     MRLTQGCFSF LPDLTDEQIS RQIQYCLDKG WAVNLEYTDD PHPRNTYWEM WGLPMFDIRD
     AKAIMSELAD CRRIHDDCYI RLSAFDATNT WESLRISFIV QRPKDEPGFM LTRSEAAGRT
     MRYETRAYVV QKPEGARYGN SG
//