RK16_SPIOL
ID RK16_SPIOL Reviewed; 135 AA.
AC P17353; Q9M3J7;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=50S ribosomal protein L16, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01342, ECO:0000303|PubMed:10874046};
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL16c {ECO:0000303|PubMed:28007896};
DE AltName: Full=Ribosomal protein CS-L24;
GN Name=rpl16 {ECO:0000255|HAMAP-Rule:MF_01342};
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].
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 1-14, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP AND METHYLATION AT MET-1.
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 -!- PTM: Partially alpha-N-monomethylated at Met-1 (10%), whereas 90% of it
CC is blocked to Edman degradation, probably by trimethylation.
CC {ECO:0000305|PubMed:10874046}.
CC -!- MASS SPECTROMETRY: Mass=15467.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC {ECO:0000255|HAMAP-Rule:MF_01342}.
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DR EMBL; X13336; CAA31716.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88765.1; -; Genomic_DNA.
DR PIR; S01979; R5SP16.
DR RefSeq; NP_054972.1; NC_002202.1.
DR PDB; 4V61; EM; 9.40 A; BO=1-135.
DR PDB; 5H1S; EM; 3.50 A; O=1-135.
DR PDB; 5MLC; EM; 3.90 A; O=1-135.
DR PDB; 5MMI; EM; 3.25 A; N=1-135.
DR PDB; 5MMM; EM; 3.40 A; N=1-135.
DR PDB; 5X8P; EM; 3.40 A; N=1-135.
DR PDB; 5X8T; EM; 3.30 A; N=1-135.
DR PDB; 6ERI; EM; 3.00 A; AM=1-134.
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; P17353; -.
DR SMR; P17353; -.
DR IntAct; P17353; 1.
DR STRING; 3562.P17353; -.
DR iPTMnet; P17353; -.
DR GeneID; 2715623; -.
DR KEGG; soe:2715623; -.
DR OrthoDB; 1510587at2759; -.
DR EvolutionaryTrace; P17353; -.
DR Proteomes; UP000054095; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR CDD; cd01433; Ribosomal_L16_L10e; 1.
DR Gene3D; 3.90.1170.10; -; 1.
DR HAMAP; MF_01342; Ribosomal_L16; 1.
DR InterPro; IPR016180; Ribosomal_L10e/L16.
DR InterPro; IPR036920; Ribosomal_L10e/L16_sf.
DR InterPro; IPR000114; Ribosomal_L16.
DR InterPro; IPR020798; Ribosomal_L16_CS.
DR PANTHER; PTHR12220; PTHR12220; 1.
DR Pfam; PF00252; Ribosomal_L16; 1.
DR PRINTS; PR00060; RIBOSOMALL16.
DR SUPFAM; SSF54686; SSF54686; 1.
DR TIGRFAMs; TIGR01164; rplP_bact; 1.
DR PROSITE; PS00586; RIBOSOMAL_L16_1; 1.
DR PROSITE; PS00701; RIBOSOMAL_L16_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Methylation; Plastid;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..135
FT /note="50S ribosomal protein L16, chloroplastic"
FT /id="PRO_0000062315"
FT MOD_RES 1
FT /note="N-methylmethionine"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CONFLICT 58
FT /note="A -> G (in Ref. 1; CAA31716)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="A -> D (in Ref. 1; CAA31716)"
FT /evidence="ECO:0000305"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 44..58
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 135 AA; 15298 MW; 908A446567467290 CRC64;
MLSPKRTRFR KQHRGRMKGI SYRGNRICFG RYALQALEPA WITSRQIEAG RRAMTRNARR
GGKIWVRIFP DKPVTVRPAE TRMGSGKGSP EYWVAVVKPG RILYEISGVA ENIARRAVAI
AASKMPIRTQ FIISG
