RK19_SPIOL
ID RK19_SPIOL Reviewed; 233 AA.
AC P82413; A0A0K9QR20; Q9M4W1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=50S ribosomal protein L19, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=CL19;
DE AltName: Full=Chloroplastic large ribosomal subunit protein bL19c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL19; Synonyms=PRPL19; ORFNames=SOVF_150800;
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 [MRNA], PROTEIN SEQUENCE OF 78-102; 200-214 AND
RP 226-233, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
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 [2]
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 [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 -!- MASS SPECTROMETRY: Mass=17566.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family.
CC {ECO:0000255}.
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DR EMBL; KQ165118; KNA09749.1; -; Genomic_DNA.
DR EMBL; AF250384; AAF64312.1; -; mRNA.
DR PDB; 4V61; EM; 9.40 A; BR=1-233.
DR PDB; 5H1S; EM; 3.50 A; R=78-233.
DR PDB; 5MLC; EM; 3.90 A; R=1-233.
DR PDB; 5MMI; EM; 3.25 A; Q=1-233.
DR PDB; 5MMM; EM; 3.40 A; Q=1-233.
DR PDB; 5X8P; EM; 3.40 A; Q=78-233.
DR PDB; 5X8T; EM; 3.30 A; Q=78-233.
DR PDB; 6ERI; EM; 3.00 A; AP=115-232.
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; P82413; -.
DR SMR; P82413; -.
DR IntAct; P82413; 1.
DR STRING; 3562.P82413; -.
DR OrthoDB; 1387536at2759; -.
DR EvolutionaryTrace; P82413; -.
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:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 2.30.30.790; -; 1.
DR InterPro; IPR038657; L19_sf.
DR InterPro; IPR001857; Ribosomal_L19.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR15680; PTHR15680; 1.
DR Pfam; PF01245; Ribosomal_L19; 1.
DR PRINTS; PR00061; RIBOSOMALL19.
DR SUPFAM; SSF50104; SSF50104; 1.
DR TIGRFAMs; TIGR01024; rplS_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..77
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 78..233
FT /note="50S ribosomal protein L19, chloroplastic"
FT /id="PRO_0000249233"
FT HELIX 119..137
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:5H1S"
FT STRAND 163..173
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:5H1S"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 233 AA; 26080 MW; 62CC200F4019E392 CRC64;
MASKVLPQAL LVIPSNHSLQ CPPLKKQLGF PIDSNRRFSL SSNCRSNLMV SRASSNLFSS
NFSSIFSFPA RNSFVVRSEA EDSSDAPAES VAVVAEEELP VESEAEAEER PPRQQRVKLG
DIMGILNKKA VHAAEELRPV PGIRTGDIVQ IRLEVPENKR RLSVYKGIVI SRQNAGIHTT
IRIRRIIAGV GVEIVFPLYS PNIKEIKVVS HRKVRKARLY YLRDKLPRLS TFK
