ID B4VHV8_9CYAN Unreviewed; 116 AA.
AC B4VHV8;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 Synonyms=rbcS {ECO:0000256|HAMAP-Rule:MF_00859};
GN ORFNames=MC7420_7420 {ECO:0000313|EMBL:EDX78767.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX78767.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX78767.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX78767.1,
RC ECO:0000313|Proteomes:UP000003835};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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 in the photorespiration process. Both reactions occur
CC simultaneously and in competition at the same active site. Although the
CC small subunit is not catalytic it is essential for maximal activity.
CC {ECO:0000256|HAMAP-Rule:MF_00859}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00859}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {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; DS989841; EDX78767.1; -; Genomic_DNA.
DR RefSeq; WP_006098244.1; NZ_DS989841.1.
DR AlphaFoldDB; B4VHV8; -.
DR STRING; 118168.MC7420_7420; -.
DR eggNOG; COG4451; Bacteria.
DR HOGENOM; CLU_098114_2_0_3; -.
DR OrthoDB; 9788955at2; -.
DR Proteomes; UP000003835; Unassembled WGS sequence.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
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 PRINTS; PR00152; RUBISCOSMALL.
DR SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; RuBisCO, small subunit; 1.
PE 3: Inferred from homology;
KW Bacterial microcompartment {ECO:0000256|HAMAP-Rule:MF_00859};
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}; Carboxysome {ECO:0000256|HAMAP-Rule:MF_00859};
KW Photorespiration {ECO:0000256|HAMAP-Rule:MF_00859};
KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00859};
KW Reference proteome {ECO:0000313|Proteomes:UP000003835}.
FT DOMAIN 9..106
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
SQ SEQUENCE 116 AA; 13684 MW; 7E6D650B005DE4CA CRC64;
MQTLPKERRY ETLSYLPPLS DQQIVRQIEY ILDQGYIPAI EFSETSEPTQ HYWTMWKLPL
FNATSPKEVM AEVDACRSDY RDNYIRVVGF DNIKQCQVLS FIIYKPGEGG RSRGYY
//
