RK4_SPIOL
ID RK4_SPIOL Reviewed; 293 AA.
AC O49937; A0A0K9RVQ9; O49938;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=50S ribosomal protein L4, chloroplastic {ECO:0000303|PubMed:10874046};
DE Short=R-protein L4;
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL4c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL4; ORFNames=SOVF_029280;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 51-63, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Melody; TISSUE=Leaf;
RX PubMed=9461586; DOI=10.1074/jbc.273.7.3980;
RA Trifa Y., Privat I., Gagnon J., Baeza L., Lerbs-Mache S.;
RT "The nuclear RPL4 gene encodes a chloroplast protein that co-purifies with
RT the T7-like transcription complex as well as plastid ribosomes.";
RL J. Biol. Chem. 273:3980-3985(1998).
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 51-68; 82-86; 98-105; 131-137; 152-158; 211-224 AND
RP 228-235, SUBUNIT, SUBCELLULAR LOCATION, 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 the
RT 50S subunit of an organelle ribosome (chloroplast).";
RL J. Biol. Chem. 275:28466-28482(2000).
RN [4]
RP CHARACTERIZATION OF TRANSCRIPTION TERMINATION ON THE SPINACH RRN OPERON.
RX PubMed=10852486; DOI=10.1007/s004380051212;
RA Trifa Y., Lerbs-Mache S.;
RT "Extra-ribosomal function(s) of the plastid ribosomal protein L4 in the
RT expression of ribosomal components in spinach.";
RL Mol. Gen. Genet. 263:642-647(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 -!- TISSUE SPECIFICITY: Highly expressed in cotyledon and weakly in roots.
CC {ECO:0000269|PubMed:9461586}.
CC -!- MASS SPECTROMETRY: Mass=27235.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- MISCELLANEOUS: This protein (expressed without the transit peptide) is
CC able to provoke transcription termination from the spinach chloroplast
CC rDNA operon and the E.coli S10 operon in vitro.
CC {ECO:0000305|PubMed:10852486}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000305}.
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DR EMBL; Y14932; CAA75149.1; -; Genomic_DNA.
DR EMBL; X93160; CAA63651.1; -; mRNA.
DR EMBL; KQ134976; KNA22937.1; -; Genomic_DNA.
DR PIR; T09170; T09170.
DR PIR; T09171; T09171.
DR PDB; 4V61; EM; 9.40 A; BG=1-293.
DR PDB; 5H1S; EM; 3.50 A; G=51-293.
DR PDB; 5MLC; EM; 3.90 A; F=1-293.
DR PDB; 5MMI; EM; 3.25 A; E=1-293.
DR PDB; 5MMM; EM; 3.40 A; E=1-293.
DR PDB; 5X8P; EM; 3.40 A; E=51-293.
DR PDB; 5X8T; EM; 3.30 A; E=51-293.
DR PDB; 6ERI; EM; 3.00 A; AE=51-262.
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; O49937; -.
DR SMR; O49937; -.
DR IntAct; O49937; 1.
DR STRING; 3562.O49937; -.
DR EvolutionaryTrace; O49937; -.
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; IBA:GO_Central.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.40.1370.10; -; 1.
DR HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR InterPro; IPR002136; Ribosomal_L4/L1e.
DR InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR InterPro; IPR013005; Ribosomal_uL4/L1e.
DR PANTHER; PTHR10746; PTHR10746; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; SSF52166; 1.
DR TIGRFAMs; TIGR03953; rplD_bact; 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; Transcription; Transcription regulation;
KW Transcription termination; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046,
FT ECO:0000269|PubMed:9461586"
FT CHAIN 51..293
FT /note="50S ribosomal protein L4, chloroplastic"
FT /id="PRO_0000030539"
FT REGION 107..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..293
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 77
FT /note="P -> S (in Ref. 2; KNA22937)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="K -> T (in Ref. 2; KNA22937)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="G -> R (in Ref. 2; KNA22937)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="E -> G (in Ref. 1; CAA63651)"
FT /evidence="ECO:0000305"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:5X8T"
FT HELIX 154..167
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 293 AA; 32435 MW; 875C425F090826E5 CRC64;
MATSTSSSLS LSFFSSSLFS SKSRNFSSKP ILKLPSSSHS QTSLSLSIKS ELIPLPILNF
SGEKVGETFL NLKTAPPEKA RAVVHRGLIT HLQNKRRGTA STLTRAEVRG GGRKPYPQKK
TGRARRGSQG SPLRPGGGVI FGPKPRDWTI KMNKKERRLA LSTAIASAVG NSFVVEEFAE
NFEKPKTKDF IAAMQRWGLD PAEKSLFFLM DLVENVEKSG RNIRTLKLLT PRSLNLFDVL
NAEKLVFTEG TIQYLNQRYG VDTLEDEDEE EEEEEEGEEV DDGVEDGTPE PAE
