RK20_SPIOL
ID RK20_SPIOL Reviewed; 128 AA.
AC P28803; Q9M3K6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=50S ribosomal protein L20, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=Chloroplastic large ribosomal subunit protein bL20c {ECO:0000303|PubMed:28007896};
GN Name=rpl20;
OS Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [2]
RP PROTEIN SEQUENCE OF 2-27.
RC STRAIN=cv. Alwaro;
RX PubMed=1421149; DOI=10.1007/bf00040605;
RA Schmidt J., Herfurth E., Subramanian A.R.;
RT "Purification and characterization of seven chloroplast ribosomal proteins:
RT evidence that organelle ribosomal protein genes are functional and that
RT NH2-terminal processing occurs via multiple pathways in chloroplasts.";
RL Plant Mol. Biol. 20:459-465(1992).
RN [3]
RP PROTEIN SEQUENCE OF 2-9, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Alwaro; TISSUE=Leaf;
RX PubMed=10874046; DOI=10.1074/jbc.m005012200;
RA Yamaguchi K., Subramanian A.R.;
RT "The plastid ribosomal proteins. Identification of all the proteins in the
RT 50S subunit of an organelle ribosome (chloroplast).";
RL J. Biol. Chem. 275:28466-28482(2000).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.4 ANGSTROMS).
RX PubMed=18042701; DOI=10.1073/pnas.0709856104;
RA Sharma M.R., Wilson D.N., Datta P.P., Barat C., Schluenzen F., Fucini P.,
RA Agrawal R.K.;
RT "Cryo-EM study of the spinach chloroplast ribosome reveals the structural
RT and functional roles of plastid-specific ribosomal proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19315-19320(2007).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS).
RX PubMed=27762343; DOI=10.1038/srep35793;
RA Ahmed T., Yin Z., Bhushan S.;
RT "Cryo-EM structure of the large subunit of the spinach chloroplast
RT ribosome.";
RL Sci. Rep. 6:35793-35793(2016).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.25 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=28007896; DOI=10.15252/embj.201695959;
RA Bieri P., Leibundgut M., Saurer M., Boehringer D., Ban N.;
RT "The complete structure of the chloroplast 70S ribosome in complex with
RT translation factor pY.";
RL EMBO J. 36:475-486(2017).
CC -!- FUNCTION: Component of the chloroplast ribosome (chloro-ribosome), a
CC dedicated translation machinery responsible for the synthesis of
CC chloroplast genome-encoded proteins, including proteins of the
CC transcription and translation machinery and components of the
CC photosynthetic apparatus. {ECO:0000305|PubMed:10874046,
CC ECO:0000305|PubMed:28007896}.
CC -!- SUBUNIT: Component of the chloroplast large ribosomal subunit (LSU).
CC Mature 70S chloroplast ribosomes of higher plants consist of a small
CC (30S) and a large (50S) subunit. The 30S small subunit contains 1
CC molecule of ribosomal RNA (16S rRNA) and 24 different proteins. The 50S
CC large subunit contains 3 rRNA molecules (23S, 5S and 4.5S rRNA) and 33
CC different proteins. {ECO:0000269|PubMed:10874046,
CC ECO:0000269|PubMed:28007896}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10874046, ECO:0000269|PubMed:28007896}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family.
CC {ECO:0000305}.
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DR EMBL; AJ400848; CAB88751.1; -; Genomic_DNA.
DR PIR; S26228; S26228.
DR RefSeq; NP_054958.1; NC_002202.1.
DR PDB; 4V61; EM; 9.40 A; BS=1-119.
DR PDB; 5H1S; EM; 3.50 A; S=2-128.
DR PDB; 5MLC; EM; 3.90 A; S=1-128.
DR PDB; 5MMI; EM; 3.25 A; R=1-128.
DR PDB; 5MMM; EM; 3.40 A; R=1-128.
DR PDB; 5X8P; EM; 3.40 A; R=2-128.
DR PDB; 5X8T; EM; 3.30 A; R=2-128.
DR PDB; 6ERI; EM; 3.00 A; AQ=2-116.
DR PDBsum; 4V61; -.
DR PDBsum; 5H1S; -.
DR PDBsum; 5MLC; -.
DR PDBsum; 5MMI; -.
DR PDBsum; 5MMM; -.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8T; -.
DR PDBsum; 6ERI; -.
DR AlphaFoldDB; P28803; -.
DR SMR; P28803; -.
DR IntAct; P28803; 1.
DR STRING; 3562.P28803; -.
DR GeneID; 2715626; -.
DR KEGG; soe:2715626; -.
DR OrthoDB; 1582185at2759; -.
DR EvolutionaryTrace; P28803; -.
DR Proteomes; UP000054095; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd07026; Ribosomal_L20; 1.
DR Gene3D; 1.10.1900.20; -; 1.
DR HAMAP; MF_00382; Ribosomal_L20; 1.
DR InterPro; IPR005813; Ribosomal_L20.
DR InterPro; IPR035566; Ribosomal_protein_L20_C.
DR PANTHER; PTHR10986; PTHR10986; 1.
DR Pfam; PF00453; Ribosomal_L20; 1.
DR PRINTS; PR00062; RIBOSOMALL20.
DR SUPFAM; SSF74731; SSF74731; 1.
DR TIGRFAMs; TIGR01032; rplT_bact; 1.
DR PROSITE; PS00937; RIBOSOMAL_L20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10874046,
FT ECO:0000269|PubMed:1421149"
FT CHAIN 2..128
FT /note="50S ribosomal protein L20, chloroplastic"
FT /id="PRO_0000177312"
FT CONFLICT 16
FT /note="K -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 19..23
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 32..70
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5X8T"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 128 AA; 15689 MW; 79926508C9A03EEB CRC64;
MTRVKRGYIA RRRRKKIRFF ASSFRGAHSR LTRTIAQQKI RALVSAHRDR DRQKRDFRRL
WITRINAAIR ERGVYYNYSK FIHDLYKRQL LLNRKILAQI AILNPNCIYM IYNEIIKKED
CKKYLEII
