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Database: UniProt
Entry: Q9LWB5
LinkDB: Q9LWB5
Original site: Q9LWB5 
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   10-MAY-2017, entry version 78.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; Caryophyllales; Chenopodiaceae; Chenopodioideae;
OC   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
RT   protein 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.,
RA   Reinhardt R., Goesmann A., Kraft T., Schulz B., Stadler P.F.,
RA   Schmidt T., Gabaldon T., 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
RT   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
RT   the 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.,
RA   Fucini P., Agrawal R.K.;
RT   "Cryo-EM study of the spinach chloroplast ribosome reveals the
RT   structural and functional roles of plastid-specific ribosomal
RT   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
RP   SUBCELLULAR 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
RT   with translation factor pY.";
RL   EMBO J. 36:475-486(2017).
CC   -!- FUNCTION: Component of the chloroplast ribosome (chloro-ribosome),
CC       a 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
CC       (LSU). Mature 70S chloroplast ribosomes of higher plants consist
CC       of a small (30S) and a large (50S) subunit. The 30S small subunit
CC       contains 1 molecule of ribosomal RNA (16S rRNA) and 24 different
CC       proteins. The 50S large subunit contains 3 rRNA molecules (23S, 5S
CC       and 4.5S rRNA) and 33 different proteins.
CC       {ECO:0000269|PubMed:10874046, 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; Range=77-
CC       198; Evidence={ECO:0000269|PubMed:10874046};
CC   -!- MISCELLANEOUS: Two forms of the protein exist; they have the same
CC       N-terminal sequence and approximately the same molecular weight.
CC       {ECO:0000269|PubMed:8021938}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL23
CC       family. {ECO:0000305}.
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   PDBsum; 4V61; -.
DR   PDBsum; 5H1S; -.
DR   PDBsum; 5MLC; -.
DR   PDBsum; 5MMI; -.
DR   PDBsum; 5MMM; -.
DR   ProteinModelPortal; Q9LWB5; -.
DR   SMR; 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: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; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   HAMAP; MF_01369_A; Ribosomal_L23_A; 1.
DR   InterPro; IPR012678; Ribosomal_L23/L15e_core_dom.
DR   InterPro; IPR013025; Ribosomal_L25/23.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; SSF54189; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Complete proteome;
KW   Direct protein sequencing; Plastid; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   Transit peptide.
FT   TRANSIT       1     76       Chloroplast.
FT                                {ECO:0000269|PubMed:10874046,
FT                                ECO:0000269|PubMed:8021938}.
FT   CHAIN        77    198       50S ribosomal protein L23, chloroplastic.
FT                                /FTId=PRO_5000146571.
FT   CONFLICT     83     83       P -> L (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     93     93       P -> N (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    101    101       K -> I (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    108    108       I -> V (in Ref. 3; AA sequence and 2;
FT                                KNA14201). {ECO:0000305}.
FT   CONFLICT    171    171       T -> TE (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    178    178       L -> I (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    189    193       KKIGI -> TEASK (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   HELIX       111    113       {ECO:0000244|PDB:5MMI}.
FT   STRAND      115    118       {ECO:0000244|PDB:5MMI}.
FT   HELIX       122    131       {ECO:0000244|PDB:5MMI}.
FT   STRAND      133    138       {ECO:0000244|PDB:5MMI}.
FT   HELIX       144    154       {ECO:0000244|PDB:5MMI}.
FT   STRAND      161    166       {ECO:0000244|PDB:5MMI}.
FT   STRAND      172    177       {ECO:0000244|PDB:5MMI}.
FT   STRAND      180    182       {ECO:0000244|PDB:5MMI}.
FT   HELIX       184    191       {ECO:0000244|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
//
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