RK14_SPIOL
ID RK14_SPIOL Reviewed; 121 AA.
AC P09596; Q9M3J8;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=50S ribosomal protein L14, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01367, ECO:0000303|PubMed:10874046};
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL14c {ECO:0000303|PubMed:28007896};
DE AltName: Full=Ribosomal protein CS-L29;
GN Name=rpl14 {ECO:0000255|HAMAP-Rule:MF_01367};
OS Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-16.
RC TISSUE=Leaf;
RX PubMed=2747623; DOI=10.1007/bf00334388;
RA Zhou D.X., Quigley F., Massenet O., Mache R.;
RT "Cotranscription of the S10- and spc-like operons in spinach chloroplasts
RT and identification of three of their gene products.";
RL Mol. Gen. Genet. 216:439-445(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-10, 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 [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., 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 [5]
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 [6]
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=13463.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC {ECO:0000255|HAMAP-Rule:MF_01367}.
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DR EMBL; X13336; CAA31717.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88764.1; -; Genomic_DNA.
DR PIR; S01980; R5SP14.
DR RefSeq; NP_054971.1; NC_002202.1.
DR PDB; 4V61; EM; 9.40 A; BM=1-121.
DR PDB; 5H1S; EM; 3.50 A; M=1-121.
DR PDB; 5MLC; EM; 3.90 A; M=1-121.
DR PDB; 5MMI; EM; 3.25 A; L=1-121.
DR PDB; 5MMM; EM; 3.40 A; L=1-121.
DR PDB; 5X8P; EM; 3.40 A; L=1-121.
DR PDB; 5X8T; EM; 3.30 A; L=1-121.
DR PDB; 6ERI; EM; 3.00 A; AK=1-121.
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; P09596; -.
DR SMR; P09596; -.
DR IntAct; P09596; 1.
DR STRING; 3562.P09596; -.
DR GeneID; 2715622; -.
DR KEGG; soe:2715622; -.
DR OrthoDB; 1547267at2759; -.
DR EvolutionaryTrace; P09596; -.
DR Proteomes; UP000054095; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.150.20; -; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1.
DR InterPro; IPR036853; Ribosomal_L14_sf.
DR InterPro; IPR000218; Ribosomal_L14P.
DR InterPro; IPR005745; Ribosomal_L14P_bac-type.
DR InterPro; IPR019972; Ribosomal_L14P_CS.
DR PANTHER; PTHR11761; PTHR11761; 1.
DR Pfam; PF00238; Ribosomal_L14; 1.
DR SMART; SM01374; Ribosomal_L14; 1.
DR SUPFAM; SSF50193; SSF50193; 1.
DR TIGRFAMs; TIGR01067; rplN_bact; 1.
DR PROSITE; PS00049; RIBOSOMAL_L14; 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.
FT CHAIN 1..121
FT /note="50S ribosomal protein L14, chloroplastic"
FT /id="PRO_0000128600"
FT CONFLICT 85
FT /note="V -> VV (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 15..27
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 121 AA; 13465 MW; 1C81677D2A35EC22 CRC64;
MIQPQTHLNV ADNSGARELM CIRIIGASNR RYARIGDVIV AVIKEAIPNT PLERSEVIRA
VVVRTCKELK RDNGMIIRYD DNAAVIIDQE GNPKGTRIFG AIARELRQKF AKIVSLAPEV
L
