RK11_SPIOL
ID RK11_SPIOL Reviewed; 224 AA.
AC P31164; A0A0K9RPN0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=50S ribosomal protein L11, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=CL11;
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL11c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=rpl11; ORFNames=SOVF_048900;
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].
RC STRAIN=cv. Matador; TISSUE=Leaf;
RX PubMed=1764529; DOI=10.1016/0300-9084(91)90064-8;
RA Smooker P.M., Schmidt J., Subramanian A.R.;
RT "The nuclear:organelle distribution of chloroplast ribosomal proteins
RT genes. Features of a cDNA clone encoding the cytoplasmic precursor of
RT L11.";
RL Biochimie 73:845-851(1991).
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 67-72, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND METHYLATION AT LYS-75 AND LYS-111.
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 (3.25 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=16749.1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000305}.
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DR EMBL; X56615; CAA39950.1; -; mRNA.
DR EMBL; KQ138260; KNA20797.1; -; Genomic_DNA.
DR PIR; S23238; R5SP11.
DR PDB; 4V61; EM; 9.40 A; BK=1-224.
DR PDB; 5MMI; EM; 3.25 A; J=1-224.
DR PDB; 5MMM; EM; 3.40 A; J=1-224.
DR PDBsum; 4V61; -.
DR PDBsum; 5MMI; -.
DR PDBsum; 5MMM; -.
DR AlphaFoldDB; P31164; -.
DR SMR; P31164; -.
DR STRING; 3562.P31164; -.
DR OrthoDB; 1346532at2759; -.
DR EvolutionaryTrace; P31164; -.
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:0015934; C: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; IBA:GO_Central.
DR CDD; cd00349; Ribosomal_L11; 1.
DR Gene3D; 1.10.10.250; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR InterPro; IPR006519; Ribosomal_L11_bac-typ.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR036769; Ribosomal_L11_C_sf.
DR InterPro; IPR020785; Ribosomal_L11_CS.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR TIGRFAMs; TIGR01632; L11_bact; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Methylation; Plastid;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 67..224
FT /note="50S ribosomal protein L11, chloroplastic"
FT /id="PRO_0000030442"
FT MOD_RES 75
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:10874046"
FT MOD_RES 111
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:10874046"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 192..206
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 224 AA; 23659 MW; A9D72639F831F58E CRC64;
MAQPLVAAPS SSSITSPIPR KLCSSLLTPS SLSLSSNPRN SLQFLNSKLF LSPPSTSHRR
LSIVAMAPKP GKAKKVIGVI KLALEAGKAT PAPPVGPALG SKGVNIMAFC KDYNARTADK
PGFVIPVEIT VFDDKSFTFI LKTPPASVLL LKASGAEKGS KDPQMEKVGK ITIDQLRGIA
TEKLPDLNCT TIESAMRIIA GTAANMGIDI DPPILVKKKK EVIF
