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RK17_SPIOL
ID   RK17_SPIOL              Reviewed;         126 AA.
AC   P82194; A0A0K9RLJ4;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 2.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=50S ribosomal protein L17, chloroplastic {ECO:0000303|PubMed:10874046};
DE   AltName: Full=CL17;
DE   AltName: Full=Chloroplastic large ribosomal subunit protein bL17c {ECO:0000303|PubMed:28007896};
DE   Flags: Precursor;
GN   Name=RPL17; ORFNames=SOVF_059230;
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 11-32, 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=13022.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10874046};
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family.
CC       {ECO:0000255}.
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DR   EMBL; KQ140075; KNA19692.1; -; Genomic_DNA.
DR   PDB; 4V61; EM; 9.40 A; P=23-32.
DR   PDB; 5H1S; EM; 3.50 A; P=11-126.
DR   PDB; 5MLC; EM; 3.90 A; P=1-126.
DR   PDB; 5MMI; EM; 3.25 A; O=1-126.
DR   PDB; 5MMM; EM; 3.40 A; O=1-126.
DR   PDB; 5X8P; EM; 3.40 A; O=11-126.
DR   PDB; 5X8T; EM; 3.30 A; O=11-126.
DR   PDB; 6ERI; EM; 3.00 A; AN=11-126.
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; P82194; -.
DR   SMR; P82194; -.
DR   IntAct; P82194; 1.
DR   STRING; 3562.P82194; -.
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: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; 3.90.1030.10; -; 1.
DR   HAMAP; MF_01368; Ribosomal_L17; 1.
DR   InterPro; IPR000456; Ribosomal_L17.
DR   InterPro; IPR036373; Ribosomal_L17_sf.
DR   PANTHER; PTHR14413; PTHR14413; 1.
DR   Pfam; PF01196; Ribosomal_L17; 1.
DR   SUPFAM; SSF64263; SSF64263; 1.
DR   TIGRFAMs; TIGR00059; L17; 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..10
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:10874046"
FT   CHAIN           11..126
FT                   /note="50S ribosomal protein L17, chloroplastic"
FT                   /id="PRO_0000249230"
FT   HELIX           24..41
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          42..47
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           48..67
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           70..77
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           83..96
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   TURN            97..100
FT                   /evidence="ECO:0007829|PDB:5H1S"
FT   STRAND          105..110
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          120..125
FT                   /evidence="ECO:0007829|PDB:5MMI"
SQ   SEQUENCE   126 AA;  14544 MW;  4E31F663C2706EEC CRC64;
     MIDNGGRFFA MKHGRKIHRL SRPADQRRAL LRGLTTQLLK HGRIKTTRAK ASAMRKYVDK
     MITLAKEGSL HKRRQALGFI YEKQIVHALF AEVPERYGDR NGGYTRIIRT LPRRGDNAPM
     AYIELV
 
 
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