RK23_SPIOL
ID RK23_SPIOL Reviewed; 198 AA.
AC Q9LWB5; A0A0K9R3X1; Q9T2N4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=50S ribosomal protein L23, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL23c {ECO:0000303|PubMed:28007896};
DE AltName: Full=PRPL23;
DE Flags: Precursor;
GN Name=RPL23; ORFNames=SOVF_109700;
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].
RC STRAIN=cv. Matador;
RA Jayabaskaran C., Subramanian A.R.;
RT "Nucleotide sequence of the cDNA coding for chloroplast ribosomal protein
RT L23 of spinach.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
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 PROTEIN SEQUENCE OF 77-113; 122-136 AND 156-193, IDENTIFICATION AS A
RP SUBUNIT OF THE CHLOROPLAST RIBOSOME, AND DEMONSTRATION OF TWO FORMS.
RC STRAIN=cv. Alwaro; TISSUE=Leaf;
RX PubMed=8021938; DOI=10.1006/jmbi.1994.1415;
RA Bubunenko M.G., Schmidt J., Subramanian A.R.;
RT "Protein substitution in chloroplast ribosome evolution. A eukaryotic
RT cytosolic protein has replaced its organelle homologue (L23) in spinach.";
RL J. Mol. Biol. 240:28-41(1994).
RN [4]
RP PROTEIN SEQUENCE OF 77-82, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP 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 [5]
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 [6]
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 [7]
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=13553.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- MISCELLANEOUS: Two forms of the protein exist; they have the same N-
CC terminal sequence and approximately the same molecular weight.
CC {ECO:0000269|PubMed:8021938}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000305}.
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DR EMBL; X90414; CAA62040.1; -; mRNA.
DR EMBL; KQ150936; KNA14201.1; -; Genomic_DNA.
DR PDB; 4V61; EM; 9.40 A; BV=1-198.
DR PDB; 5H1S; EM; 3.50 A; V=77-198.
DR PDB; 5MLC; EM; 3.90 A; V=1-198.
DR PDB; 5MMI; EM; 3.25 A; U=1-198.
DR PDB; 5MMM; EM; 3.40 A; U=1-198.
DR PDB; 5X8P; EM; 3.40 A; U=77-198.
DR PDB; 5X8T; EM; 3.30 A; U=77-198.
DR PDB; 6ERI; EM; 3.00 A; AT=103-194.
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; Q9LWB5; -.
DR SMR; Q9LWB5; -.
DR IntAct; Q9LWB5; 1.
DR STRING; 3562.Q9LWB5; -.
DR PRIDE; Q9LWB5; -.
DR EvolutionaryTrace; Q9LWB5; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProt.
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:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_01369_A; Ribosomal_L23_A; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR11620; PTHR11620; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR SUPFAM; SSF54189; SSF54189; 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..76
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046,
FT ECO:0000269|PubMed:8021938"
FT CHAIN 77..198
FT /note="50S ribosomal protein L23, chloroplastic"
FT /id="PRO_5000146571"
FT CONFLICT 83
FT /note="P -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="P -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="K -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="I -> V (in Ref. 3; AA sequence and 2; KNA14201)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="T -> TE (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="L -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..193
FT /note="KKIGI -> TEASK (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 198 AA; 21800 MW; 624DF1D4032BB70F CRC64;
MATTAPNLHS LSSSFAFSNP SSNVSATSFT FQIPNKKAQI SCISSKKLHT QKSFNFHDAV
TPMNKPSFGR DLMVAQATEA VAPTTEEAAT SQPKTSKKAK KLKYPRRILD VYQILQSPII
TEAAIKNIAD ENSLLFTVDV RADKKMIREA ISNFFGVKVR KVNTLIRPDG TKKAYIMLNK
EYNASELAKK IGIFPGGN
