ID RK23_SPIOL Reviewed; 198 AA.
AC Q9LWB5; Q9T2N4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-APR-2013, entry version 62.
DE RecName: Full=50S ribosomal protein L23, chloroplastic;
DE AltName: Full=PRPL23;
DE Flags: Precursor;
GN Name=RPL23;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC Caryophyllales; Amaranthaceae; 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 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 [3]
RP PROTEIN SEQUENCE OF 77-82, 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
RT the 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.,
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).
CC -!- FUNCTION: Binds to 23S rRNA (By similarity). Located at the
CC polypeptide exit tunnel on the outside of the subunit.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- MASS SPECTROMETRY: Mass=13553.5; Method=Electrospray; Range=77-
CC 198; Source=PubMed:10874046;
CC -!- MISCELLANEOUS: This protein is the 80S cytosolic ortholog and is
CC imported into the plastid, unlike the case in most plastids where
CC it is the bacterial ortholog and is encoded in the plastid. Two
CC forms of the protein exist; they have the same N-terminal sequence
CC and approximately the same molecular weight.
CC -!- SIMILARITY: Belongs to the ribosomal protein L23P family.
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DR EMBL; X90414; CAA62040.1; -; mRNA.
DR PDB; 3BBO; EM; 9.40 A; V=1-198.
DR PDBsum; 3BBO; -.
DR ProteinModelPortal; Q9LWB5; -.
DR SMR; Q9LWB5; 110-194.
DR EvolutionaryTrace; Q9LWB5; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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 Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR SUPFAM; SSF54189; L23_L15e_core; 1.
DR PROSITE; PS00050; RIBOSOMAL_L23; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Plastid;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Transit peptide.
FT TRANSIT 1 76 Chloroplast.
FT CHAIN 77 198 50S ribosomal protein L23, chloroplastic.
FT /FTId=PRO_5000146571.
FT CONFLICT 83 83 P -> L (in Ref. 2; AA sequence).
FT CONFLICT 93 93 P -> N (in Ref. 2; AA sequence).
FT CONFLICT 101 101 K -> I (in Ref. 2; AA sequence).
FT CONFLICT 108 108 I -> V (in Ref. 2; AA sequence).
FT CONFLICT 171 171 T -> TE (in Ref. 2; AA sequence).
FT CONFLICT 178 178 L -> I (in Ref. 2; AA sequence).
FT CONFLICT 189 193 KKIGI -> TEASK (in Ref. 2; AA sequence).
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
//
