RK15_SPIOL
ID RK15_SPIOL Reviewed; 271 AA.
AC P22798; A0A0K9QHT0;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 3.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=50S ribosomal protein L15, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=CL15;
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL15c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL15; ORFNames=SOVF_177460;
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 62-91; 122-141; 157-171; 185-199 AND 249-259.
RC STRAIN=cv. Alwaro;
RX PubMed=2037044; DOI=10.1016/0014-5793(91)80492-l;
RA Johnson C.H., Subramanian A.R.;
RT "Chloroplast ribosomal protein L15, like L1, L13 and L21, is significantly
RT larger than its E. coli homologue.";
RL FEBS Lett. 282:268-272(1991).
RN [3]
RP PROTEIN SEQUENCE OF 62-67, 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 STRUCTURE BY ELECTRON MICROSCOPY (9.40 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 -!- MASS SPECTROMETRY: Mass=22327.9; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 family.
CC {ECO:0000305}.
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DR EMBL; KQ180134; KNA06817.1; -; Genomic_DNA.
DR PIR; S15817; S15817.
DR PDB; 4V61; EM; 9.40 A; N=77-259.
DR PDB; 5H1S; EM; 3.50 A; N=80-271.
DR PDB; 5MLC; EM; 3.90 A; N=1-271.
DR PDB; 5MMI; EM; 3.25 A; M=1-271.
DR PDB; 5MMM; EM; 3.40 A; M=1-271.
DR PDB; 5X8P; EM; 3.40 A; M=80-271.
DR PDB; 5X8T; EM; 3.30 A; M=80-271.
DR PDB; 6ERI; EM; 3.00 A; AL=78-261.
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; P22798; -.
DR SMR; P22798; -.
DR IntAct; P22798; 1.
DR STRING; 3562.P22798; -.
DR PRIDE; P22798; -.
DR OrthoDB; 930708at2759; -.
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:0003729; F:mRNA binding; IEA:UniProt.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR HAMAP; MF_01341; Ribosomal_L15; 1.
DR InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR030878; Ribosomal_L15.
DR InterPro; IPR005749; Ribosomal_L15_bac-type.
DR InterPro; IPR001196; Ribosomal_L15_CS.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR PANTHER; PTHR12934; PTHR12934; 1.
DR Pfam; PF00828; Ribosomal_L27A; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR TIGRFAMs; TIGR01071; rplO_bact; 1.
DR PROSITE; PS00475; RIBOSOMAL_L15; 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..61
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 62..271
FT /note="50S ribosomal protein L15, chloroplastic"
FT /id="PRO_0000104878"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5X8T"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5H1S"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:5H1S"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:5X8T"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:5H1S"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5H1S"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5X8T"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5H1S"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5H1S"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 244..261
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 271 AA; 29030 MW; 2310AEE56EE592D8 CRC64;
MASLLSLSST PPSTANSNNY PSSTFKGNIN NFRINPFNFA PLKLHLRNIV KKESTRLVVV
ASASSSNVSP SIGSGSETRF RLDNLGPQPG SRKKGKRKGR GHAAGQGGSC GFGMRGQKSR
SGPGIMRGFE GGQMPLYRRI PKLRGIAGGM RAGLPKYVPI NLRDIEVAGF KEGEEVSLES
LKAKGIINPS GRERRLPLKI LGEGELSTKL QIKARAFSGS AKEKLEAAGC SVTVLPGRKK
YIKESVRKNL ARADEYFAKK RAASASEAES A
