RK27_SPIOL
ID RK27_SPIOL Reviewed; 194 AA.
AC P82190; A0A0K9R4I2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=50S ribosomal protein L27, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=CL27;
DE AltName: Full=Chloroplastic large ribosomal subunit protein bL27c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL27; ORFNames=SOVF_107450;
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 58-115, 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=13650.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family.
CC {ECO:0000255}.
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DR EMBL; KQ150476; KNA14420.1; -; Genomic_DNA.
DR PDB; 4V61; EM; 9.40 A; X=58-115.
DR PDB; 5H1S; EM; 3.50 A; X=58-194.
DR PDB; 5MLC; EM; 3.90 A; X=1-194.
DR PDB; 5MMI; EM; 3.25 A; X=1-194.
DR PDB; 5MMM; EM; 3.40 A; X=1-194.
DR PDB; 5X8P; EM; 3.40 A; X=58-194.
DR PDB; 5X8T; EM; 3.30 A; X=58-194.
DR PDB; 6ERI; EM; 3.00 A; AW=60-173.
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; P82190; -.
DR SMR; P82190; -.
DR IntAct; P82190; 1.
DR STRING; 3562.P82190; -.
DR OrthoDB; 1177118at2759; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR HAMAP; MF_00539; Ribosomal_L27; 1.
DR InterPro; IPR001684; Ribosomal_L27.
DR InterPro; IPR018261; Ribosomal_L27_CS.
DR PANTHER; PTHR15893; PTHR15893; 1.
DR Pfam; PF01016; Ribosomal_L27; 1.
DR PRINTS; PR00063; RIBOSOMALL27.
DR TIGRFAMs; TIGR00062; L27; 1.
DR PROSITE; PS00831; RIBOSOMAL_L27; 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..57
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 58..194
FT /note="50S ribosomal protein L27, chloroplastic"
FT /id="PRO_0000249406"
FT REGION 57..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 115..127
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 150..167
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 194 AA; 21329 MW; 7BB90273E8A5A944 CRC64;
MAVTTSMSFN LMASFRGMSL SSSSSSSFFK GEFGPSSLRL PNKSPLSVSP FPLTIESAHK
KGAGSTKNGR DSKGQRLGVK IYGDQVAKPG AIIIRQRGTK FHPGKNVGIG KDHTIFALID
GLVKFEKYGP DKKKVSVYPR EIQPENPNSY RARKRENFRL QREKKKARRE GYSFQPQLIL
ASAATDNADE SAVC
