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Database: UniProt
Entry: P82244
LinkDB: P82244
Original site: P82244 
ID   RK34_SPIOL              Reviewed;         152 AA.
AC   P82244; A0A0K9RGW2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2000, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Large ribosomal subunit protein bL34c {ECO:0000303|PubMed:28007896};
DE   AltName: Full=50S ribosomal protein L34, chloroplastic {ECO:0000303|PubMed:10874046};
DE   AltName: Full=CL34;
DE   Flags: Precursor;
GN   Name=RPL34; ORFNames=SOVF_073030;
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 [MRNA], PROTEIN SEQUENCE OF 92-101, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND MASS 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   [2]
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   [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=6939.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10874046};
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family.
CC       {ECO:0000305}.
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DR   EMBL; AF238221; AAF64157.1; -; mRNA.
DR   EMBL; KQ142564; KNA18199.1; -; Genomic_DNA.
DR   PDB; 4V61; EM; 9.40 A; B4=1-152.
DR   PDB; 5H1S; EM; 3.50 A; d=92-151.
DR   PDB; 5MLC; EM; 3.90 A; 4=1-152.
DR   PDB; 5MMI; EM; 3.25 A; 3=1-152.
DR   PDB; 5MMM; EM; 3.40 A; 3=1-152.
DR   PDB; 5X8P; EM; 3.40 A; 3=92-152.
DR   PDB; 5X8T; EM; 3.30 A; 3=92-152.
DR   PDB; 6ERI; EM; 3.00 A; Ac=92-152.
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; P82244; -.
DR   EMDB; EMD-3525; -.
DR   EMDB; EMD-3531; -.
DR   EMDB; EMD-3533; -.
DR   EMDB; EMD-3941; -.
DR   EMDB; EMD-6709; -.
DR   EMDB; EMD-6711; -.
DR   EMDB; EMD-9572; -.
DR   SMR; P82244; -.
DR   IntAct; P82244; 1.
DR   STRING; 3562.P82244; -.
DR   OrthoDB; 1131370at2759; -.
DR   EvolutionaryTrace; P82244; -.
DR   Proteomes; UP001155700; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005762; C:mitochondrial 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; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 1.10.287.3980; -; 1.
DR   HAMAP; MF_00391; Ribosomal_bL34; 1.
DR   InterPro; IPR000271; Ribosomal_bL34.
DR   NCBIfam; TIGR01030; rpmH_bact; 1.
DR   PANTHER; PTHR14503:SF14; 50S RIBOSOMAL PROTEIN L34, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR14503; MITOCHONDRIAL RIBOSOMAL PROTEIN 34 FAMILY MEMBER; 1.
DR   Pfam; PF00468; Ribosomal_L34; 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..91
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:10874046"
FT   CHAIN           92..152
FT                   /note="Large ribosomal subunit protein bL34c"
FT                   /id="PRO_0000030519"
FT   HELIX           96..99
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           105..109
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           114..117
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           121..133
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          145..149
FT                   /evidence="ECO:0007829|PDB:5MMI"
SQ   SEQUENCE   152 AA;  16096 MW;  755A990D441ADB18 CRC64;
     MATLSLLSTG VGAAITNRTP SASLTFITGS RTTNKRVSFN GGSARSGSLH CSFLAPSSSL
     SSNFSGLSLG LDLTSNTGVS TDRCRRFVVR AGKAALCLTK RSRSRKSLAR THGFRLRMST
     TSGRALLKRR RAKGRKILCT KTNPSSGKRA SP
//
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