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RBS4_SOLLC
ID   RBS4_SOLLC              Reviewed;         180 AA.
AC   P05349;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 4 {ECO:0000255|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit 4 {ECO:0000255|HAMAP-Rule:MF_00860};
DE   AltName: Full=Ribulose bisphosphate carboxylase small chain 3B, chloroplastic {ECO:0000303|PubMed:3478552};
DE            Short=RuBisCO small subunit 3B {ECO:0000303|PubMed:3478552};
DE   Flags: Precursor;
GN   Name=RBCS4 {ECO:0000255|HAMAP-Rule:MF_00860};
GN   Synonyms=RBCS-3B {ECO:0000303|PubMed:3478552};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. VFNT Cherry LA1221;
RX   PubMed=3478552; DOI=10.1007/bf00329650;
RA   Sugita M., Manzara T., Pichersky E., Cashmore A., Gruissem W.;
RT   "Genomic organization, sequence analysis and expression of all five genes
RT   encoding the small subunit of ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase from tomato.";
RL   Mol. Gen. Genet. 209:247-256(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC   STRAIN=cv. VFNT Cherry LA1221; TISSUE=Root;
RX   PubMed=8425051; DOI=10.1007/bf00039619;
RA   Manzara T., Carrasco P., Gruissem W.;
RT   "Developmental and organ-specific changes in DNA-protein interactions in
RT   the tomato rbcS1, rbcS2 and rbcS3A promoter regions.";
RL   Plant Mol. Biol. 21:69-88(1993).
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. Involved in antiviral defenses (By
CC       similarity). {ECO:0000250|UniProtKB:A0A0S4IJL0, ECO:0000255|HAMAP-
CC       Rule:MF_00860}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00860}.
CC   -!- SUBUNIT: (Microbial infection) Binds to tobamovirus movement protein;
CC       this interaction seems required for viral systemic movement.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_00860}.
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}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00860}.
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DR   EMBL; D11112; BAA01888.1; -; Genomic_DNA.
DR   EMBL; X05985; CAA29403.1; -; Genomic_DNA.
DR   EMBL; X66071; CAA46871.1; -; Genomic_DNA.
DR   PIR; S01107; RKTO3B.
DR   RefSeq; NP_001296139.1; NM_001309210.1.
DR   RefSeq; XP_019067516.1; XM_019211971.1.
DR   AlphaFoldDB; P05349; -.
DR   SMR; P05349; -.
DR   STRING; 4081.Solyc02g085950.2.1; -.
DR   PaxDb; P05349; -.
DR   PRIDE; P05349; -.
DR   EnsemblPlants; Solyc02g085950.3.1; Solyc02g085950.3.1; Solyc02g085950.3.
DR   GeneID; 101268337; -.
DR   Gramene; Solyc02g085950.3.1; Solyc02g085950.3.1; Solyc02g085950.3.
DR   KEGG; sly:101268337; -.
DR   eggNOG; ENOG502QT0M; Eukaryota.
DR   HOGENOM; CLU_098114_1_0_1; -.
DR   InParanoid; P05349; -.
DR   OMA; RKNWVPC; -.
DR   OrthoDB; 1258997at2759; -.
DR   PhylomeDB; P05349; -.
DR   Proteomes; UP000004994; Chromosome 2.
DR   ExpressionAtlas; P05349; baseline and differential.
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   3: Inferred from homology;
KW   Antiviral defense; Calvin cycle; Carbon dioxide fixation; Cell junction;
KW   Chloroplast; Host-virus interaction; Photorespiration; Photosynthesis;
KW   Plastid; Reference proteome; Transit peptide.
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 4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031521"
SQ   SEQUENCE   180 AA;  20213 MW;  AD77A593B7AC8512 CRC64;
     MASSIVSSAA VATRGNGAQA SMVAPFTGLK STASFPVSRK QNLDITSIAS NGGRVSCMQV
     WPPINMKKYE TLSYLPDLSD EQLLSEIEYL LKNGWVPCLE FETEHGFVYR ENHKSPGYYD
     GRYWTMWKLP MFGCTDATQV LAEVQEAKKA YPQAWVRIIG FDNVRQVQCI SFIAYKPEGY
 
 
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