RK29_SPIOL
ID RK29_SPIOL Reviewed; 168 AA.
AC P82248; A0A0K9R7W8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=50S ribosomal protein L29, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=CL29;
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL29c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL29; ORFNames=SOVF_096810;
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 {ECO:0000305};
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 59-84, 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=13502.1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL29 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ147688; KNA15596.1; -; Genomic_DNA.
DR PDB; 4V61; EM; 9.40 A; Z=64-79.
DR PDB; 5H1S; EM; 3.50 A; Z=60-168.
DR PDB; 5MLC; EM; 3.90 A; Z=1-168.
DR PDB; 5MMI; EM; 3.25 A; Z=1-168.
DR PDB; 5MMM; EM; 3.40 A; Z=1-168.
DR PDB; 5X8P; EM; 3.40 A; Z=60-168.
DR PDB; 5X8T; EM; 3.30 A; Z=60-168.
DR PDB; 6ERI; EM; 3.00 A; AY=59-157.
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; P82248; -.
DR SMR; P82248; -.
DR IntAct; P82248; 1.
DR STRING; 3562.P82248; -.
DR OrthoDB; 1508529at2759; -.
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; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 1.10.287.310; -; 1.
DR HAMAP; MF_00374; Ribosomal_L29; 1.
DR InterPro; IPR001854; Ribosomal_L29/L35.
DR InterPro; IPR036049; Ribosomal_L29/L35_sf.
DR Pfam; PF00831; Ribosomal_L29; 1.
DR SUPFAM; SSF46561; SSF46561; 1.
DR TIGRFAMs; TIGR00012; L29; 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..58
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 59..168
FT /note="50S ribosomal protein L29, chloroplastic"
FT /id="PRO_0000130532"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 75
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 73..96
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 103..126
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 168 AA; 19046 MW; 176C2ECCC5943207 CRC64;
MLAIHSLSST PCSSGLTSPP KSTLLTKSSF HGLRLPSVNL SSSLRLRVQT PPSSVVVMVK
KEDELKELRT KTNEQLNEEI LQLKGELFML RLQRSARENF KPSDFGRMRK RVARMLTVKR
EREIEQGVGK RLSRKLDKAW KRSIVVRPPP SLKKLQEKAT AEAEAEKA
