RBS_SYNE7
ID RBS_SYNE7 Reviewed; 111 AA.
AC Q31NB2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
GN Synonyms=rbcS {ECO:0000255|HAMAP-Rule:MF_00859,
GN ECO:0000303|PubMed:17675289}; OrderedLocusNames=Synpcc7942_1427;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CCMM, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=17675289; DOI=10.1074/jbc.m703896200;
RA Long B.M., Badger M.R., Whitney S.M., Price G.D.;
RT "Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple
RT Rubisco complexes with carboxysomal proteins CcmM and CcaA.";
RL J. Biol. Chem. 282:29323-29335(2007).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=22928045; DOI=10.1371/journal.pone.0043871;
RA Rae B.D., Long B.M., Badger M.R., Price G.D.;
RT "Structural determinants of the outer shell of beta-carboxysomes in
RT Synechococcus elongatus PCC 7942: roles for CcmK2, K3-K4, CcmO, and CcmL.";
RL PLoS ONE 7:e43871-e43871(2012).
RN [4]
RP CARBOXYSOME ASSEMBLY PROCESS, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=24267892; DOI=10.1016/j.cell.2013.10.044;
RA Cameron J.C., Wilson S.C., Bernstein S.L., Kerfeld C.A.;
RT "Biogenesis of a bacterial organelle: the carboxysome assembly pathway.";
RL Cell 155:1131-1140(2013).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=24585024; DOI=10.1007/s11120-014-9986-7;
RA Nishimura T., Yamaguchi O., Takatani N., Maeda S., Omata T.;
RT "In vitro and in vivo analyses of the role of the carboxysomal beta-type
RT carbonic anhydrase of the cyanobacterium Synechococcus elongatus in
RT carboxylation of ribulose-1,5-bisphosphate.";
RL Photosyn. Res. 121:151-157(2014).
RN [6]
RP RUBISCO FOLDING AND ASSEMBLY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=26237510; DOI=10.1038/nsmb.3062;
RA Hauser T., Bhat J.Y., Milicic G., Wendler P., Hartl F.U., Bracher A.,
RA Hayer-Hartl M.;
RT "Structure and mechanism of the Rubisco-assembly chaperone Raf1.";
RL Nat. Struct. Mol. Biol. 22:720-728(2015).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=28616951; DOI=10.1039/c7nr02524f;
RA Faulkner M., Rodriguez-Ramos J., Dykes G.F., Owen S.V., Casella S.,
RA Simpson D.M., Beynon R.J., Liu L.N.;
RT "Direct characterization of the native structure and mechanics of
RT cyanobacterial carboxysomes.";
RL Nanoscale 9:10662-10673(2017).
RN [8]
RP BIOTECHNOLOGY.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=29922315; DOI=10.3389/fpls.2018.00739;
RA Fang Y., Huang F., Faulkner M., Jiang Q., Dykes G.F., Yang M., Liu L.N.;
RT "Engineering and Modulating Functional Cyanobacterial CO2-Fixing
RT Organelles.";
RL Front. Plant Sci. 9:739-739(2018).
RN [9]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=31048338; DOI=10.1105/tpc.18.00787;
RA Sun Y., Wollman A.J.M., Huang F., Leake M.C., Liu L.N.;
RT "Single-Organelle Quantification Reveals Stoichiometric and Structural
RT Variability of Carboxysomes Dependent on the Environment.";
RL Plant Cell 31:1648-1664(2019).
RN [10]
RP CARBOXYSOME ASSEMBLY PROCESS, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=32636267; DOI=10.1073/pnas.2007990117;
RA Huang F., Kong W.W., Sun Y., Chen T., Dykes G.F., Jiang Y.L., Liu L.N.;
RT "Rubisco accumulation factor 1 (Raf1) plays essential roles in mediating
RT Rubisco assembly and carboxysome biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:17418-17428(2020).
RN [11] {ECO:0007744|PDB:6HBC}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.78 ANGSTROMS) IN COMPLEX WITH LARGE
RP SUBUNIT AND CCMM35, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=30675061; DOI=10.1038/s41586-019-0880-5;
RA Wang H., Yan X., Aigner H., Bracher A., Nguyen N.D., Hee W.Y., Long B.M.,
RA Price G.D., Hartl F.U., Hayer-Hartl M.;
RT "Rubisco condensate formation by CcmM in beta-carboxysome biogenesis.";
RL Nature 566:131-135(2019).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|PubMed:24585024,
CC ECO:0000269|PubMed:30675061}.
CC -!- FUNCTION: Beta-carboxysome assembly initiates when soluble RuBisCO
CC aggregates is condensed into a liquid matrix in a pre-carboxysome by
CC the RbcS-like domains of probably both CcmM58 and CcmM35. CcmN
CC interacts with the N-terminus of CcmM58, and then recruits the CcmK2
CC major shell protein via CcmN's encapsulation peptide. Shell formation
CC requires CcmK proteins and CcmO. CcmL caps the otherwise elongated
CC carboxysome. Once fully encapsulated carboxysomes are formed, they
CC migrate within the cell probably via interactions with the
CC cytoskeleton. {ECO:0000269|PubMed:24267892,
CC ECO:0000269|PubMed:30675061}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits (Probable).
CC The CcmM short form purifies from carboxysomes in complex with both
CC RuBisCO subunits; a second complex with full-length CcmM and RuBisCO
CC also includes carbonic anhydrase (CA, ccaA). RuBisCO-CcmM complexes are
CC probably associated with the carboxysome shell (PubMed:17675289).
CC Isolated reduced and oxidized SSUL1 binds holo-RuBisCO (RbcL(8)-
CC RbcS(8)) but not either subunit octamer alone; RuBisCO has a higher
CC affinity for reduced SSUL1 (PubMed:30675061).
CC {ECO:0000269|PubMed:17675289, ECO:0000269|PubMed:30675061,
CC ECO:0000305|PubMed:26237510, ECO:0000305|PubMed:30675061}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00859,
CC ECO:0000269|PubMed:17675289, ECO:0000269|PubMed:22928045,
CC ECO:0000269|PubMed:24585024, ECO:0000269|PubMed:28616951,
CC ECO:0000269|PubMed:31048338, ECO:0000269|PubMed:32636267,
CC ECO:0000305|PubMed:24267892}. Note=In the carboxysome RuBisCO is
CC organized into a paracrystalline array (PubMed:28616951). This
CC cyanobacterium makes beta-type carboxysomes (PubMed:22928045).
CC {ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:28616951}.
CC -!- INDUCTION: Carboxysome size and components vary with growth conditions.
CC When grown in ambient air at medium light (50 uE meter(-2) second(-1))
CC there are 853 RuBisCO complexes (RbcL8S8) per carboxysome, the numbers
CC decrease under low light and high CO(2), and increase under high light
CC (at protein level). {ECO:0000269|PubMed:31048338}.
CC -!- BIOTECHNOLOGY: Heterologous expression of 12 carboxysomal genes in
CC E.coli (ccaA, ccmK2, ccmK3, ccmK4, ccmL, ccmM, ccmN, ccmO, ccmP, rbcL,
CC rbcS, rbcX) leads to the formation of bodies that resemble
CC carboxysomes, have densely packed paracrystalline arrays and RuBisCO
CC activity. These structures open the door to generating carboxysomes in
CC plant cells to increase their photosynthesis and productivity, as well
CC as tailoring bacterial microcompartments to specific metabolic needs
CC and molecule delivery. {ECO:0000269|PubMed:29922315}.
CC -!- MISCELLANEOUS: RuBisCO folding and assembly commences when the nascent
CC large subunit folds with the help of chaperonin GroEL-GroES. Both RbcX
CC and Raf1 help folded RbcL release from the chaperonin and dimerize;
CC dimeric Raf1 binds to RbcL(2) leading to an RbcL8-Raf1(8) complex. RbcS
CC displaces Raf1, resulting in holoenzyme formation.
CC {ECO:0000269|PubMed:26237510, ECO:0000305|PubMed:32636267}.
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; CP000100; ABB57457.1; -; Genomic_DNA.
DR PDB; 6HBC; EM; 2.78 A; D/E=1-111.
DR PDBsum; 6HBC; -.
DR AlphaFoldDB; Q31NB2; -.
DR SMR; Q31NB2; -.
DR STRING; 1140.Synpcc7942_1427; -.
DR PRIDE; Q31NB2; -.
DR EnsemblBacteria; ABB57457; ABB57457; Synpcc7942_1427.
DR KEGG; syf:Synpcc7942_1427; -.
DR eggNOG; COG4451; Bacteria.
DR HOGENOM; CLU_098114_2_0_3; -.
DR OMA; KQCQVLS; -.
DR BioCyc; SYNEL:SYNPCC7942_1427-MON; -.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
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 3D-structure; Bacterial microcompartment; Calvin cycle;
KW Carbon dioxide fixation; Carboxysome; Photorespiration; Photosynthesis.
FT CHAIN 1..111
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /id="PRO_0000451248"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:6HBC"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:6HBC"
SQ SEQUENCE 111 AA; 13333 MW; F854F73FA70BD57B CRC64;
MSMKTLPKER RFETFSYLPP LSDRQIAAQI EYMIEQGFHP LIEFNEHSNP EEFYWTMWKL
PLFDCKSPQQ VLDEVRECRS EYGDCYIRVA GFDNIKQCQT VSFIVHRPGR Y
