RK13_SPIOL
ID RK13_SPIOL Reviewed; 250 AA.
AC P12629; A0A0K9RAG3;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=50S ribosomal protein L13, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=CL13;
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL13c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL13; ORFNames=SOVF_093170;
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 [MRNA].
RX PubMed=2644249; DOI=10.1016/s0021-9258(18)94129-3;
RA Phua S.H., Srinivasa B.R., Subramanian A.R.;
RT "Chloroplast ribosomal protein L13 is encoded in the nucleus and is
RT considerably larger than its bacterial homologue. Construction,
RT immunoisolation, and nucleotide sequence (including transit peptide) its
RT cDNA clone from an angiosperm.";
RL J. Biol. Chem. 264:1968-1971(1989).
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 48-53, 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 FUNCTION.
RX PubMed=1879566; DOI=10.1016/0014-5793(91)81005-s;
RA Giese K., Subramanian A.R.;
RT "Expression and functional assembly into bacterial ribosomes of a nuclear-
RT encoded chloroplast ribosomal protein with a long NH2-terminal extension.";
RL FEBS Lett. 288:72-76(1991).
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 -!- MASS SPECTROMETRY: Mass=23365.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC {ECO:0000305}.
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DR EMBL; J04461; AAA34040.1; -; mRNA.
DR EMBL; KQ146763; KNA15999.1; -; Genomic_DNA.
DR PIR; A32033; A32033.
DR PDB; 4V61; EM; 9.40 A; BL=1-250.
DR PDB; 5H1S; EM; 3.50 A; L=60-250.
DR PDB; 5MLC; EM; 3.90 A; L=1-250.
DR PDB; 5MMI; EM; 3.25 A; K=1-250.
DR PDB; 5MMM; EM; 3.40 A; K=1-250.
DR PDB; 5X8P; EM; 3.40 A; K=54-250.
DR PDB; 5X8T; EM; 3.30 A; K=54-250.
DR PDB; 6ERI; EM; 3.00 A; AJ=49-248.
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; P12629; -.
DR SMR; P12629; -.
DR IntAct; P12629; 1.
DR STRING; 3562.P12629; -.
DR OrthoDB; 1119705at2759; -.
DR EvolutionaryTrace; P12629; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00392; Ribosomal_L13; 1.
DR Gene3D; 3.90.1180.10; -; 1.
DR HAMAP; MF_01366; Ribosomal_L13; 1.
DR InterPro; IPR005822; Ribosomal_L13.
DR InterPro; IPR005823; Ribosomal_L13_bac-type.
DR InterPro; IPR023563; Ribosomal_L13_CS.
DR InterPro; IPR036899; Ribosomal_L13_sf.
DR PANTHER; PTHR11545; PTHR11545; 1.
DR Pfam; PF00572; Ribosomal_L13; 1.
DR SUPFAM; SSF52161; SSF52161; 1.
DR TIGRFAMs; TIGR01066; rplM_bact; 1.
DR PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 48..250
FT /note="50S ribosomal protein L13, chloroplastic"
FT /id="PRO_0000030461"
FT HELIX 53..72
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5X8T"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 250 AA; 28164 MW; 0B8F157B7A948EA7 CRC64;
MATMACASSL TFPSAQTQKS FFGTNVKQTP VLSFPRPTVA AAVAVSARKS TSASTKCTEE
WRQLKEAVKK EFAIPHVPLD QRWMFTLEEA TGPDIWNTTW YPKSADHVPT DKKWYVVDAT
DLILGRMAST IAIHIRGKNL ASYTPSVDMG AFVIVVNADK VAVSGKKRTQ KLYRRHSGRP
GGLKEETFDQ LQKRIPERII EHAVRGMLPK GRLGRYLFNH LKVYKGAEHP HQAQQPIDLP
LRDKRIRVEK