ID RBS_RHIME Reviewed; 129 AA. AC P58349; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 16-NOV-2001, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000255|HAMAP-Rule:MF_00859}; DE Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00859}; GN Name=cbbS {ECO:0000255|HAMAP-Rule:MF_00859}; OrderedLocusNames=RB0190; GN ORFNames=SMb20197; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OG Plasmid pSymB (megaplasmid 2). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11481431; DOI=10.1073/pnas.161294698; RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J., RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.; RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing RT endosymbiont Sinorhizobium meliloti."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11474104; DOI=10.1126/science.1060966; RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., RA Wong K., Yeh K.-C., Batut J.; RT "The composite genome of the legume symbiont Sinorhizobium meliloti."; RL Science 293:668-672(2001). 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 -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits. CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00859}. CC -!- SIMILARITY: Belongs to the RuBisCO small chain family. CC {ECO:0000255|HAMAP-Rule:MF_00859}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL591985; CAC48590.1; -; Genomic_DNA. DR PIR; F95865; F95865. DR RefSeq; NP_436730.1; NC_003078.1. DR RefSeq; WP_010975099.1; NC_003078.1. DR AlphaFoldDB; P58349; -. DR SMR; P58349; -. DR EnsemblBacteria; CAC48590; CAC48590; SM_b20197. DR GeneID; 61600205; -. DR KEGG; sme:SM_b20197; -. DR PATRIC; fig|266834.11.peg.5106; -. DR eggNOG; COG4451; Bacteria. DR HOGENOM; CLU_098114_2_0_5; -. DR OrthoDB; 9788955at2; -. DR Proteomes; UP000001976; Plasmid pSymB. 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; Carbon dioxide fixation; Plasmid; Reference proteome. FT CHAIN 1..129 FT /note="Ribulose bisphosphate carboxylase small subunit" FT /id="PRO_0000198619" FT REGION 109..129 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 110..129 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 129 AA; 15147 MW; B3A4DF100179F3FE CRC64; MRITQGCFSF LPDLTDEQIT AQVQYCLGKG WAIGVEYTDD PHPRNTYWEM WGNPMFDLKD AKGVMMELED CRKAHPQDYI RLNAFDSSRG LETVTMSFIV NRPENEPSLR MTRTESNGRS QHYMWETQR //