RK5_SPIOL
ID RK5_SPIOL Reviewed; 258 AA.
AC P82192; A0A0K9RJX4; Q9M4W0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 3.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=50S ribosomal protein L5, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL5c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL5; Synonyms=PrpL5; ORFNames=SOVF_057730;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-258, PROTEIN SEQUENCE OF 39-63, SUBUNIT,
RP 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 [3]
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 [4]
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 [5]
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}.
CC -!- MASS SPECTROMETRY: Mass=24207.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
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DR EMBL; KQ139872; KNA19821.1; -; Genomic_DNA.
DR EMBL; AF250923; AAF64313.1; -; mRNA.
DR PDB; 4V61; EM; 9.40 A; BH=39-258.
DR PDB; 5H1S; EM; 3.50 A; H=39-258.
DR PDB; 5MLC; EM; 3.90 A; G=39-258.
DR PDB; 5MMI; EM; 3.25 A; F=1-258.
DR PDB; 5MMM; EM; 3.40 A; F=1-258.
DR PDB; 5X8P; EM; 3.40 A; F=39-258.
DR PDB; 5X8T; EM; 3.30 A; F=39-258.
DR PDB; 6ERI; EM; 3.00 A; AF=52-258.
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; P82192; -.
DR SMR; P82192; -.
DR IntAct; P82192; 1.
DR STRING; 3562.P82192; -.
DR EvolutionaryTrace; P82192; -.
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:0003723; F:RNA binding; IBA:GO_Central.
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:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.1440.10; -; 1.
DR HAMAP; MF_01333_B; Ribosomal_L5_B; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR020930; Ribosomal_L5_bac-type.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR020929; Ribosomal_L5_CS.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
DR PROSITE; PS00358; RIBOSOMAL_L5; 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; Transit peptide.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 39..258
FT /note="50S ribosomal protein L5, chloroplastic"
FT /id="PRO_0000125048"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 158..163
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:5H1S"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5H1S"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 258 AA; 28140 MW; 52C18B2D224AFF4C CRC64;
MASTSLLQST SSSFAGVRFH CRTSAAPRVG LSSFTVKAAA GTAVFVDKAE AETINRLKTN
YIEKMVPLLK EEFSYSNILE VPKVVKIVVN CGIGDASQNA KGLDAAINEL ALITGQRPVK
TKAKTSIAGF KVREGMTLGI AVTLRGNLMY SFLDRLINLA LPRTRDFQGV NPNSFDGHGN
YSVGFREQSV FPEIKPEIVG KARGMDVCIT TTAKTDKEAY KLLSLMGMPF REGSGPSTLV
RKKKLKSHHF DAKKGRRY
