RBS_NICBE
ID RBS_NICBE Reviewed; 180 AA.
AC A0A0S4IJL0; A0A4P8WEX4;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000303|PubMed:23148080};
DE Short=NbRbCS {ECO:0000303|PubMed:23148080};
DE Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000303|PubMed:23148080};
DE Flags: Precursor;
GN Name=rbcS {ECO:0000303|Ref.1, ECO:0000303|Ref.2};
OS Nicotiana benthamiana.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4100;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Kumari R., Hallan V.;
RT "Characterization of Rubisco small chain from Nicotiana benthamiana.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu X.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), DISRUPTION PHENOTYPE, INTERACTION
RP WITH TOBACCO MOSAIC VIRUS MOVEMENT PROTEIN (MICROBIAL INFECTION), AND
RP SUBCELLULAR LOCATION.
RX PubMed=23148080; DOI=10.1104/pp.112.209213;
RA Zhao J., Liu Q., Zhang H., Jia Q., Hong Y., Liu Y.;
RT "The rubisco small subunit is involved in tobamovirus movement and Tm-2(2)-
RT mediated extreme resistance.";
RL Plant Physiol. 161:374-383(2013).
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 (By similarity). Involved in antiviral
CC defenses (PubMed:23148080). {ECO:0000255|HAMAP-Rule:MF_00860,
CC ECO:0000269|PubMed:23148080}.
CC -!- FUNCTION: (Microbial infection) Required for tobamovirus movement (e.g.
CC tobacco mosaic virus (TMV)). {ECO:0000269|PubMed:23148080}.
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 at
CC the plasmodesmata (e.g. tomato mosaic virus MP AC P69513); this
CC interaction seems required for viral systemic movement.
CC {ECO:0000269|PubMed:23148080}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:P69249, ECO:0000255|HAMAP-Rule:MF_00860}.
CC -!- SUBCELLULAR LOCATION: Cell junction, plasmodesma
CC {ECO:0000269|PubMed:23148080}. Note=(Microbial infection) May be
CC present in virus replication complexes (VRCs) of tobamovirus infected
CC cells. {ECO:0000269|PubMed:23148080}.
CC -!- DISRUPTION PHENOTYPE: In susceptible plants, increased tomato mosaic
CC tobamovirus (ToMV) induced necrosis in inoculated leaves but delayed
CC development of systemic viral symptoms (PubMed:23148080). ToMV is able
CC to establish efficient local infection but not to move systemically
CC (PubMed:23148080). Compromised Tm-2(2)-dependent resistance
CC (PubMed:23148080). {ECO:0000269|PubMed:23148080}.
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; LN877373; CUA55116.1; -; mRNA.
DR EMBL; MK070896; QCS40508.1; -; mRNA.
DR AlphaFoldDB; A0A0S4IJL0; -.
DR SMR; A0A0S4IJL0; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; IDA:UniProtKB.
DR GO; GO:0019034; C:viral replication complex; IDA:UniProtKB.
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 Antiviral defense; Calvin cycle; Carbon dioxide fixation; Cell junction;
KW Chloroplast; Photorespiration; Photosynthesis; Plastid; 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"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000448714"
FT CONFLICT 105
FT /note="H -> R (in Ref. 2; QCS40508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20342 MW; D2070C8DDB463E42 CRC64;
MASSVLSSAA VATRSNVAQA NMVAPFTGLK SAASFPVSRK QNLDITSIAS NGGRVQCMQV
WPPINKKKYE TLSYLPDLSV EQLLSEIEYL LKNGWVPCLE FETEHGFVYR EHHKSPGYYD
GRYWTMWKLP MFGCTDATQV LAEVEEAKKA YPQAWIRIIG FDNVRQVQCI SFIAYKPEGY
