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RK28_SPIOL
ID   RK28_SPIOL              Reviewed;         148 AA.
AC   P82245; A0A0K9RD02;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 2.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=50S ribosomal protein L28, chloroplastic {ECO:0000303|PubMed:10874046};
DE   AltName: Full=CL28;
DE   AltName: Full=Chloroplastic large ribosomal subunit protein bL28c {ECO:0000303|PubMed:28007896};
DE   Flags: Precursor;
GN   Name=RPL28; ORFNames=SOVF_085320;
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 72-90, 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=9071.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10874046};
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family.
CC       {ECO:0000255}.
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DR   EMBL; KQ144998; KNA16864.1; -; Genomic_DNA.
DR   PDB; 4V61; EM; 9.40 A; Y=72-90.
DR   PDB; 5H1S; EM; 3.50 A; Y=72-148.
DR   PDB; 5MLC; EM; 3.90 A; Y=1-148.
DR   PDB; 5MMI; EM; 3.25 A; Y=1-148.
DR   PDB; 5MMM; EM; 3.40 A; Y=1-148.
DR   PDB; 5X8P; EM; 3.40 A; Y=72-148.
DR   PDB; 5X8T; EM; 3.30 A; Y=72-148.
DR   PDB; 6ERI; EM; 3.00 A; AX=72-147.
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; P82245; -.
DR   SMR; P82245; -.
DR   IntAct; P82245; 1.
DR   STRING; 3562.P82245; -.
DR   OrthoDB; 1614134at2759; -.
DR   Proteomes; UP000054095; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 2.30.170.40; -; 1.
DR   HAMAP; MF_00373; Ribosomal_L28; 1.
DR   InterPro; IPR034704; L28p-like.
DR   InterPro; IPR026569; Ribo_L28/L24.
DR   InterPro; IPR037147; Ribo_L28/L24_sf.
DR   InterPro; IPR001383; Ribosomal_L28.
DR   PANTHER; PTHR13528; PTHR13528; 1.
DR   Pfam; PF00830; Ribosomal_L28; 1.
DR   SUPFAM; SSF143800; SSF143800; 1.
DR   TIGRFAMs; TIGR00009; L28; 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..71
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:10874046"
FT   CHAIN           72..148
FT                   /note="50S ribosomal protein L28, chloroplastic"
FT                   /id="PRO_0000249407"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          103..110
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   TURN            111..114
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          115..122
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           123..132
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           134..141
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   TURN            145..147
FT                   /evidence="ECO:0007829|PDB:5MMI"
SQ   SEQUENCE   148 AA;  16430 MW;  72C51FD8708A9761 CRC64;
     MAASGMLISN PSNVCFRKPQ FSCSLKPKAT VSELGFLTSQ LSGIQISPSP LFPIISKPIS
     APLKPSLQPV ARRICPFTGK KSNKANRVSH SNHKTKRLQF VNLQYKRVWW EAGKRFVKLR
     LSTKALKTIE KNGLDAVAKK AGIDLRKE
 
 
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