RBS_NOSS1
ID RBS_NOSS1 Reviewed; 109 AA.
AC P06514;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 121.
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:6091125}; OrderedLocusNames=alr1526;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=6091125; DOI=10.1073/pnas.81.19.5961;
RA Nierzwicki-Bauer S.A., Curtis S.E., Haselkorn R.;
RT "Cotranscription of genes encoding the small and large subunits of
RT ribulose-1,5-bisphosphate carboxylase in the cyanobacterium Anabaena
RT 7120.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5961-5965(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=24907906; DOI=10.1007/s11120-014-0018-4;
RA de Araujo C., Arefeen D., Tadesse Y., Long B.M., Price G.D., Rowlett R.S.,
RA Kimber M.S., Espie G.S.;
RT "Identification and characterization of a carboxysomal gamma-carbonic
RT anhydrase from the cyanobacterium Nostoc sp. PCC 7120.";
RL Photosyn. Res. 121:135-150(2014).
RN [4] {ECO:0007744|PDB:6LRR, ECO:0007744|PDB:6LRS}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS) IN COMPLEX WITH RBCL AND
RP RAF1, FUNCTION, RUBISCO FOLDING AND ASSEMBLY, AND SUBUNIT.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=32451445; DOI=10.1038/s41477-020-0665-8;
RA Xia L.Y., Jiang Y.L., Kong W.W., Sun H., Li W.F., Chen Y., Zhou C.Z.;
RT "Molecular basis for the assembly of RuBisCO assisted by the chaperone
RT Raf1.";
RL Nat. Plants 6:708-717(2020).
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:0000255|HAMAP-Rule:MF_00859, ECO:0000269|PubMed:32451445}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits
CC (PubMed:32451445). Forms complexes of many stoichiometries with Raf1
CC and RbcL (PubMed:32451445). {ECO:0000269|PubMed:32451445}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00859,
CC ECO:0000269|PubMed:24907906}. Note=This cyanobacterium makes beta-type
CC carboxysomes (PubMed:24907906). In the carboxysome RuBisCO is organized
CC into a paracrystalline array (By similarity).
CC {ECO:0000250|UniProtKB:Q31NB2, ECO:0000269|PubMed:24907906}.
CC -!- INDUCTION: Part of the rbcL-rbcS operon, transcribed in light and
CC constitutively during growth on fructose. {ECO:0000269|PubMed:6091125}.
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:32451445}.
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, ECO:0000269|PubMed:32451445}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00859}.
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DR EMBL; J01540; AAA22042.1; -; Genomic_DNA.
DR EMBL; L02520; AAA22025.1; -; Genomic_DNA.
DR EMBL; L02521; AAA22026.1; -; Genomic_DNA.
DR EMBL; L02522; AAA22030.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB77892.1; -; Genomic_DNA.
DR PIR; AH1996; AH1996.
DR RefSeq; WP_010995695.1; NZ_RSCN01000022.1.
DR PDB; 6LRR; EM; 3.37 A; Q/R/T/U/V/W/X/Y=1-109.
DR PDB; 6LRS; EM; 3.37 A; Q/R/S/T=1-109.
DR PDB; 6Z1F; EM; 2.86 A; I/J/K/L/M/N/O/P=1-109.
DR PDB; 6Z1G; EM; 8.20 A; D/E=1-109.
DR PDBsum; 6LRR; -.
DR PDBsum; 6LRS; -.
DR PDBsum; 6Z1F; -.
DR PDBsum; 6Z1G; -.
DR AlphaFoldDB; P06514; -.
DR SMR; P06514; -.
DR STRING; 103690.17135346; -.
DR EnsemblBacteria; BAB77892; BAB77892; BAB77892.
DR KEGG; ana:alr1526; -.
DR eggNOG; COG4451; Bacteria.
DR OMA; KQCQVLS; -.
DR OrthoDB; 1708389at2; -.
DR Proteomes; UP000002483; Chromosome.
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;
KW Reference proteome.
FT CHAIN 1..109
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /id="PRO_0000198610"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6LRR"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:6Z1F"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:6Z1F"
SQ SEQUENCE 109 AA; 12827 MW; 00AF32BB0A703595 CRC64;
MQTLPKERRY ETLSYLPPLT DVQIEKQVQY ILSQGYIPAV EFNEVSEPTE LYWTLWKLPL
FGAKTSREVL AEVQSCRSQY PGHYIRVVGF DNIKQCQILS FIVHKPSRY