RK18_SPIOL
ID RK18_SPIOL Reviewed; 166 AA.
AC P82195; A0A0K9QQ60; P82196;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 3.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=50S ribosomal protein L18, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=CL18;
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL18c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL18; Synonyms=PRPL18; ORFNames=SOVF_159210;
OS Spinacia oleracea (Spinach).
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. Viroflay; TISSUE=Leaf;
RX PubMed=24352233; DOI=10.1038/nature12817;
RA Dohm J.C., Minoche A.E., Holtgraewe D., Capella-Gutierrez S.,
RA Zakrzewski F., Tafer H., Rupp O., Soerensen T.R., Stracke R., Reinhardt R.,
RA Goesmann A., Kraft T., Schulz B., Stadler P.F., Schmidt T., Gabaldon T.,
RA Lehrach H., Weisshaar B., Himmelbauer H.;
RT "The genome of the recently domesticated crop plant sugar beet (Beta
RT vulgaris).";
RL Nature 505:546-549(2014).
RN [2]
RP PROTEIN SEQUENCE OF 45-73, 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 [3]
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 [4]
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 [5]
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 -!- MISCELLANEOUS: There are two forms of L18, alpha and beta, both with a
CC MW of 11.5 kDa. They probably differ by an unknown post-translational
CC modification; their first 26 amino acids are identical.
CC {ECO:0000269|PubMed:10874046}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC {ECO:0000305}.
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DR EMBL; KQ168860; KNA08833.1; -; Genomic_DNA.
DR PDB; 4V61; EM; 9.40 A; Q=45-73.
DR PDB; 5H1S; EM; 3.50 A; Q=44-166.
DR PDB; 5MLC; EM; 3.90 A; Q=1-166.
DR PDB; 5MMI; EM; 3.25 A; P=1-166.
DR PDB; 5MMM; EM; 3.40 A; P=1-166.
DR PDB; 5X8P; EM; 3.40 A; P=44-166.
DR PDB; 5X8T; EM; 3.30 A; P=44-166.
DR PDB; 6ERI; EM; 3.00 A; AO=46-166.
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; P82195; -.
DR SMR; P82195; -.
DR IntAct; P82195; 1.
DR STRING; 3562.P82195; -.
DR OrthoDB; 1400359at2759; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0008097; F:5S rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR HAMAP; MF_01337_B; Ribosomal_L18_B; 1.
DR InterPro; IPR005484; Ribosomal_L18.
DR InterPro; IPR004389; Ribosomal_L18_bac-type.
DR PANTHER; PTHR12899; PTHR12899; 1.
DR Pfam; PF00861; Ribosomal_L18p; 1.
DR TIGRFAMs; TIGR00060; L18_bact; 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; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 45..166
FT /note="50S ribosomal protein L18, chloroplastic"
FT /id="PRO_0000131429"
FT HELIX 49..63
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5H1S"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5H1S"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 166 AA; 18378 MW; 98EA5F95A30040E5 CRC64;
MAAATSLSFF HSTLASSSSS SVQQLSLPPK FVNFRPQTLP LIQAKAHTRR EDRTARHVRI
RKKVEGTPER PRLCVFRSNK HLYVQVIDDT KMHTLAAAST MQKAISENID YSAGPTVEVA
QKIGEMIAKS CLEKGITKVA FDRGGYPYHG RVKALADAAR EHGLVF
