ID   A9QPF8_METI4            Unreviewed;       140 AA.
AC   A9QPF8;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 80.
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:ABX56616.1};
GN   Synonyms=rbcS {ECO:0000313|EMBL:ACD83317.1};
GN   OrderedLocusNames=Minf_1263 {ECO:0000313|EMBL:ACD83317.1};
OS   Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS   V4)).
OC   Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC   Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX   NCBI_TaxID=481448 {ECO:0000313|EMBL:ABX56616.1};
RN   [1] {ECO:0000313|EMBL:ABX56616.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=V4 {ECO:0000313|EMBL:ABX56616.1};
RX   PubMed=18004300; DOI=10.1038/nature06411;
RA   Dunfield P.F., Yuryev A., Senin P., Smirnova A.V., Stott M.B., Hou S.,
RA   Ly B., Saw J.H., Zhou Z., Ren Y., Wang J., Mountain B.W., Crowe M.A.,
RA   Weatherby T.M., Bodelier P.L.E., Liesack W., Feng L., Wang L., Alam M.;
RT   "Methane oxidation by an extremely acidophilic bacterium of the phylum
RT   Verrucomicrobia.";
RL   Nature 450:879-882(2007).
RN   [2] {ECO:0000313|EMBL:ACD83317.1, ECO:0000313|Proteomes:UP000009149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate V4 {ECO:0000313|Proteomes:UP000009149}, and V4
RC   {ECO:0000313|EMBL:ACD83317.1};
RX   PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA   Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA   Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA   Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA   Feng L., Wang L., Alam M.;
RT   "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT   V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT   Verrucomicrobia.";
RL   Biol. Direct 3:26-26(2008).
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; EU223874; ABX56616.1; -; Genomic_DNA.
DR   EMBL; CP000975; ACD83317.1; -; Genomic_DNA.
DR   RefSeq; WP_012463599.1; NC_010794.1.
DR   AlphaFoldDB; A9QPF8; -.
DR   STRING; 481448.Minf_1263; -.
DR   KEGG; min:Minf_1263; -.
DR   eggNOG; COG4451; Bacteria.
DR   HOGENOM; CLU_098114_2_0_0; -.
DR   OrthoDB; 25430at2; -.
DR   Proteomes; UP000009149; 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   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}.
FT   DOMAIN          4..103
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   140 AA;  16717 MW;  E95FBA11AB293F95 CRC64;
     MRITQGTFSY LPDLTDEEIA AQVQYIIDQG WSIMIEYTDN PHPRHTYWDM WGLPLFDIKD
     PAAVMQELNE CRKAYPNHYI RISGYNRQQG YQTTMISFIC NRPKEEPGFE LVRTEWADRQ
     QKYQLKPYAI DKPKGQRYKS
//