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Database: UniProt
Entry: RK14_SPIOL
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Original site: 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   24-JAN-2024, entry version 125.
DE   RecName: Full=Large ribosomal subunit protein uL14c {ECO:0000303|PubMed:28007896};
DE   AltName: Full=50S ribosomal protein L14, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01367, ECO:0000303|PubMed:10874046};
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   EMDB; EMD-3525; -.
DR   EMDB; EMD-3531; -.
DR   EMDB; EMD-3533; -.
DR   EMDB; EMD-3941; -.
DR   EMDB; EMD-6709; -.
DR   EMDB; EMD-6711; -.
DR   EMDB; EMD-9572; -.
DR   SMR; P09596; -.
DR   IntAct; P09596; 1.
DR   STRING; 3562.P09596; -.
DR   GeneID; 2715622; -.
DR   KEGG; soe:2715622; -.
DR   InParanoid; P09596; -.
DR   OrthoDB; 312166at2759; -.
DR   EvolutionaryTrace; P09596; -.
DR   Proteomes; UP001155700; Chloroplast Pltd.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0022625; C:cytosolic 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; Ribosomal protein L14; 1.
DR   HAMAP; MF_01367; Ribosomal_uL14; 1.
DR   InterPro; IPR000218; Ribosomal_uL14.
DR   InterPro; IPR005745; Ribosomal_uL14_bac-type.
DR   InterPro; IPR019972; Ribosomal_uL14_CS.
DR   InterPro; IPR036853; Ribosomal_uL14_sf.
DR   NCBIfam; TIGR01067; rplN_bact; 1.
DR   PANTHER; PTHR11761; 50S/60S RIBOSOMAL PROTEIN L14/L23; 1.
DR   PANTHER; PTHR11761:SF3; 54S RIBOSOMAL PROTEIN L38, MITOCHONDRIAL; 1.
DR   Pfam; PF00238; Ribosomal_L14; 1.
DR   SMART; SM01374; Ribosomal_L14; 1.
DR   SUPFAM; SSF50193; Ribosomal protein L14; 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="Large ribosomal subunit protein uL14c"
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
//
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