RK9_SPIOL
ID RK9_SPIOL Reviewed; 196 AA.
AC P82180; A0A0K9RQ91;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=50S ribosomal protein L9, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=CL9;
DE AltName: Full=Chloroplastic large ribosomal subunit protein bL9c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL9; ORFNames=SOVF_040960;
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 PROTEIN SEQUENCE OF 42-86, 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 [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, ECO:0000269|PubMed:28007896}.
CC -!- MASS SPECTROMETRY: Mass=17674.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family.
CC {ECO:0000255}.
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DR EMBL; KQ136810; KNA21690.1; -; Genomic_DNA.
DR PDB; 4V61; EM; 9.40 A; J=46-86.
DR PDB; 5H1S; EM; 3.50 A; J=42-196.
DR PDB; 5MLC; EM; 3.90 A; I=1-196.
DR PDB; 5MMI; EM; 3.25 A; H=1-196.
DR PDB; 5MMM; EM; 3.40 A; H=1-196.
DR PDB; 5X8P; EM; 3.40 A; H=42-196.
DR PDB; 5X8T; EM; 3.30 A; H=42-196.
DR PDB; 6ERI; EM; 3.00 A; AH=43-88.
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; P82180; -.
DR SMR; P82180; -.
DR IntAct; P82180; 1.
DR STRING; 3562.P82180; -.
DR OrthoDB; 1503131at2759; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.10.430.100; -; 1.
DR Gene3D; 3.40.5.10; -; 1.
DR HAMAP; MF_00503; Ribosomal_L9; 1.
DR InterPro; IPR000244; Ribosomal_L9.
DR InterPro; IPR009027; Ribosomal_L9/RNase_H1_N.
DR InterPro; IPR020594; Ribosomal_L9_bac/chp.
DR InterPro; IPR020069; Ribosomal_L9_C.
DR InterPro; IPR036791; Ribosomal_L9_C_sf.
DR InterPro; IPR020070; Ribosomal_L9_N.
DR InterPro; IPR036935; Ribosomal_L9_N_sf.
DR PANTHER; PTHR21368; PTHR21368; 1.
DR Pfam; PF03948; Ribosomal_L9_C; 1.
DR Pfam; PF01281; Ribosomal_L9_N; 1.
DR SUPFAM; SSF55653; SSF55653; 1.
DR SUPFAM; SSF55658; SSF55658; 1.
DR TIGRFAMs; TIGR00158; L9; 1.
DR PROSITE; PS00651; RIBOSOMAL_L9; 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..41
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 42..196
FT /note="50S ribosomal protein L9, chloroplastic"
FT /id="PRO_0000249861"
FT CONFLICT 81
FT /note="L -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="E -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:5X8T"
SQ SEQUENCE 196 AA; 22002 MW; 1823DE61DD7349F8 CRC64;
MASTTSTLSL SWSNSFHSFA GAISEPQKSP ENCRVMLPIV AQKKVKKIRK IILKEDIPDL
GKKGQLLDVR AGFLRNFLLP LGKAEVVTPL LLKEMKMEDE RIEAEKKRVK EEAQQLARMF
ETVGAFKVKR KGGKGKQIFG SVTAQDLVDI IKAQLQRDVD KKVVFLPDIR ETGEYIAELK
LHPDVTAQVR VTVFAN
