RBS_TOBAC
ID RBS_TOBAC Reviewed; 180 AA.
AC P69249; P00866; P00867; P26666;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000303|PubMed:3681999};
DE Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000303|PubMed:3681999};
DE AltName: Full=TSSU3-8 {ECO:0000303|PubMed:3684569};
DE Flags: Precursor;
GN Name=RBCS {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000303|PubMed:3681999};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=4000958; DOI=10.1093/nar/13.7.2373;
RA Mazur B.J., Chui C.-F.;
RT "Sequence of a genomic DNA clone for the small subunit of ribulose bis-
RT phosphate carboxylase-oxygenase from tobacco.";
RL Nucleic Acids Res. 13:2373-2386(1985).
RN [2]
RP PROTEIN SEQUENCE OF 58-180.
RA Mueller K.-D., Salnikow J., Vater J.;
RT "Amino acid sequence of the small subunit of D-ribulose bisphosphate
RT carboxylase/oxygenase from Nicotiana tabacum.";
RL Biochim. Biophys. Acta 742:78-83(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-101.
RX PubMed=3684569; DOI=10.1093/nar/15.21.8661;
RA O'Neal J.K., Pokalsky A.R., Kiehne K.L., Shewmaker C.K.;
RT "Isolation of tobacco SSU genes: characterization of a transcriptionally
RT active pseudogene.";
RL Nucleic Acids Res. 15:8661-8677(1987).
RN [4] {ECO:0007744|PDB:4RUB}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 58-180 OF ACTIVATED HOLOENZYME,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=3681999; DOI=10.1016/0022-2836(87)90129-x;
RA Suh S.W., Cascio D., Chapman M.S., Eisenberg D.;
RT "A crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase from
RT Nicotiana tabacum in the activated state.";
RL J. Mol. Biol. 197:363-365(1987).
RN [5] {ECO:0007744|PDB:3RUB}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-180 OF UNACTIVATED HOLOENZYME,
RP AND SUBUNIT.
RC STRAIN=cv. Turkish samsun;
RX PubMed=1512238; DOI=10.1016/s0021-9258(18)41881-9;
RA Curmi P.M.G., Cascio D., Sweet R.M., Eisenberg D., Schreuder H.;
RT "Crystal structure of the unactivated form of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase from tobacco refined at 2.0-A resolution.";
RL J. Biol. Chem. 267:16980-16989(1992).
RN [6] {ECO:0007744|PDB:1EJ7}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 58-180 OF UNACTIVATED HOLOENZYME,
RP AND SUBUNIT.
RC STRAIN=cv. Wisconsin-38;
RX PubMed=10801357; DOI=10.1006/jmbi.2000.3724;
RA Duff A.P., Andrews T.J., Curmi P.M.G.;
RT "The transition between the open and closed states of rubisco is triggered
RT by the inter-phosphate distance of the bound bisphosphate.";
RL J. Mol. Biol. 298:903-916(2000).
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 (PubMed:3681999). Both reactions occur simultaneously and in
CC competition at the same active site (Probable). Involved in antiviral
CC defenses (By similarity). {ECO:0000250|UniProtKB:A0A0S4IJL0,
CC ECO:0000269|PubMed:3681999, ECO:0000305}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000269|PubMed:1512238,
CC ECO:0000269|PubMed:3681999}.
CC -!- SUBUNIT: (Microbial infection) Binds to tobamovirus movement protein;
CC this interaction seems required for viral systemic movement.
CC {ECO:0000250|UniProtKB:A0A0S4IJL0, ECO:0000305}.
CC -!- INTERACTION:
CC P69249; O81283: TOC159; Xeno; NbExp=5; IntAct=EBI-1766821, EBI-639063;
CC P69249; Q38906: TOC34; Xeno; NbExp=6; IntAct=EBI-1766821, EBI-1766808;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_00860, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell junction, plasmodesma
CC {ECO:0000250|UniProtKB:A0A0S4IJL0}. Note=(Microbial infection) May be
CC present in virus replication complexes (VRCs) of tobamovirus infected
CC cells. {ECO:0000250|UniProtKB:A0A0S4IJL0}.
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_00860, ECO:0000269|PubMed:1512238,
CC ECO:0000269|PubMed:3681999}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
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DR EMBL; X02353; CAA26208.1; -; Genomic_DNA.
DR EMBL; M32419; AAA34116.1; -; Genomic_DNA.
DR PIR; A22934; RKNTSP.
DR RefSeq; XP_016440853.1; XM_016585367.1.
DR RefSeq; XP_016481946.1; XM_016626460.1.
DR PDB; 1EJ7; X-ray; 2.45 A; S=58-180.
DR PDB; 1RLC; X-ray; 2.70 A; S=58-180.
DR PDB; 1RLD; X-ray; 2.50 A; S/T=58-180.
DR PDB; 3RUB; X-ray; 2.00 A; S=58-180.
DR PDB; 4RUB; X-ray; 2.70 A; S/T/U/V=58-180.
DR PDBsum; 1EJ7; -.
DR PDBsum; 1RLC; -.
DR PDBsum; 1RLD; -.
DR PDBsum; 3RUB; -.
DR PDBsum; 4RUB; -.
DR AlphaFoldDB; P69249; -.
DR SMR; P69249; -.
DR DIP; DIP-40635N; -.
DR IntAct; P69249; 4.
DR MINT; P69249; -.
DR STRING; 4097.P69249; -.
DR PRIDE; P69249; -.
DR GeneID; 107766567; -.
DR GeneID; 107802883; -.
DR KEGG; nta:107766567; -.
DR KEGG; nta:107802883; -.
DR OMA; KQCQVLS; -.
DR OrthoDB; 1258997at2759; -.
DR PhylomeDB; P69249; -.
DR BRENDA; 4.1.1.39; 3645.
DR SABIO-RK; P69249; -.
DR EvolutionaryTrace; P69249; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
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; IPR024680; RuBisCO_ssu_N.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR PANTHER; PTHR31262; PTHR31262; 1.
DR Pfam; PF12338; RbcS; 1.
DR Pfam; PF00101; RuBisCO_small; 1.
DR PRINTS; PR00152; RUBISCOSMALL.
DR SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; SSF55239; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Calvin cycle; Carbon dioxide fixation;
KW Cell junction; Chloroplast; Direct protein sequencing; Photorespiration;
KW Photosynthesis; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000269|Ref.2"
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT CHAIN 57..180
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000031560"
FT CONFLICT 87..88
FT /note="VE -> PD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3RUB"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:3RUB"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:3RUB"
SQ SEQUENCE 180 AA; 20311 MW; 26CF3F48EF0860AD CRC64;
MASSVLSSAA VATRSNVAQA NMVAPFTGLK SAASFPVSRK QNLDITSIAS NGGRVQCMQV
WPPINKKKYE TLSYLPDLSQ EQLLSEVEYL LKNGWVPCLE FETEHGFVYR ENNKSPGYYD
GRYWTMWKLP MFGCTDATQV LAEVEEAKKA YPQAWIRIIG FDNVRQVQCI SFIAYKPEGY
