PSRP5_SPIOL
ID PSRP5_SPIOL Reviewed; 142 AA.
AC P27684; A0A0K9S2M7; Q9M4R3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=50S ribosomal protein 5 alpha, chloroplastic {ECO:0000305};
DE AltName: Full=50S ribosomal protein L40;
DE AltName: Full=CL40;
DE AltName: Full=Chloroplastic large ribosomal subunit protein cL37 {ECO:0000303|PubMed:28007896};
DE AltName: Full=Plastid-specific 50S ribosomal protein 5 alpha {ECO:0000303|PubMed:10874046};
DE Short=PSRP-5;
DE Contains:
DE RecName: Full=50S ribosomal protein 5 beta, chloroplastic {ECO:0000303|PubMed:10874046};
DE Contains:
DE RecName: Full=50S ribosomal protein 5 gamma, chloroplastic {ECO:0000303|PubMed:10874046};
DE Flags: Precursor;
GN Name=PSRP5; Synonyms=RPL40; ORFNames=SOVF_000530;
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], AND PROTEIN SEQUENCE OF 63-74.
RX PubMed=1889743; DOI=10.1016/0378-1119(91)90266-e;
RA Carol P., Li Y.F., Mache R.;
RT "Conservation and evolution of the nucleus-encoded and chloroplast-specific
RT ribosomal proteins in pea and spinach.";
RL Gene 103:139-145(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 63-68 AND 85-98, 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 [3]
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 [4]
RP SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX PubMed=12605670; DOI=10.1046/j.1432-1033.2003.03359.x;
RA Yamaguchi K., Subramanian A.R.;
RT "Proteomic identification of all plastid-specific ribosomal proteins in
RT higher plant chloroplast 30S ribosomal subunit.";
RL Eur. J. Biochem. 270:190-205(2003).
RN [5]
RP MODELING ON THE 70S RIBOSOME, AND POSSIBLE RNA-BINDING.
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 [6]
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 [7]
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: [50S ribosomal protein 5 alpha, chloroplastic]:
CC Mass=9296.0; Method=Electrospray; Note=PSRP-5 alpha form.;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- MASS SPECTROMETRY: [50S ribosomal protein 5 alpha, chloroplastic]:
CC Mass=9255; Method=Electrospray; Note=PSRP-5 alpha form.;
CC Evidence={ECO:0000269|PubMed:12605670};
CC -!- MASS SPECTROMETRY: [50S ribosomal protein 5 beta, chloroplastic]:
CC Mass=7065.0; Method=Electrospray; Note=PSRP-5 beta form.;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- MASS SPECTROMETRY: [50S ribosomal protein 5 beta, chloroplastic]:
CC Mass=7066; Method=Electrospray; Note=PSRP-5 beta form.;
CC Evidence={ECO:0000269|PubMed:12605670};
CC -!- MASS SPECTROMETRY: [50S ribosomal protein 5 gamma, chloroplastic]:
CC Mass=6636.5; Method=Electrospray; Note=PSRP-5 gamma form.;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- MASS SPECTROMETRY: [50S ribosomal protein 5 gamma, chloroplastic]:
CC Mass=6638; Method=Electrospray; Note=PSRP-5 gamma form.;
CC Evidence={ECO:0000269|PubMed:12605670};
CC -!- MISCELLANEOUS: Three different forms exist, PSRP-5 alpha, PSRP-5 beta
CC and PSRP-5 gamma, due to different transit peptide cleavage.
CC {ECO:0000269|PubMed:10874046}.
CC -!- SIMILARITY: Belongs to the chloroplast-specific ribosomal protein cL37
CC family. {ECO:0000305}.
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DR EMBL; M58523; AAA34044.1; -; mRNA.
DR EMBL; AF261940; AAF72995.1; -; mRNA.
DR EMBL; KQ130794; KNA26006.1; -; Genomic_DNA.
DR PIR; JH0586; JH0586.
DR PDB; 5H1S; EM; 3.50 A; g=1-142.
DR PDB; 5MLC; EM; 3.90 A; 7=1-142.
DR PDB; 5MMI; EM; 3.25 A; 6=1-142.
DR PDB; 5MMM; EM; 3.40 A; 6=1-142.
DR PDB; 5X8P; EM; 3.40 A; 6=1-142.
DR PDB; 5X8T; EM; 3.30 A; 6=1-142.
DR PDB; 6ERI; EM; 3.00 A; Aw=94-142.
DR PDBsum; 5H1S; -.
DR PDBsum; 5MLC; -.
DR PDBsum; 5MMI; -.
DR PDBsum; 5MMM; -.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8T; -.
DR PDBsum; 6ERI; -.
DR AlphaFoldDB; P27684; -.
DR SMR; P27684; -.
DR IntAct; P27684; 29.
DR STRING; 3562.P27684; -.
DR OrthoDB; 1644212at2759; -.
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:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032544; P:plastid translation; IBA:GO_Central.
DR InterPro; IPR040307; 50S_RP.
DR PANTHER; PTHR34678; PTHR34678; 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..62
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046,
FT ECO:0000269|PubMed:1889743"
FT CHAIN 63..142
FT /note="50S ribosomal protein 5 alpha, chloroplastic"
FT /id="PRO_0000030555"
FT CHAIN 85..142
FT /note="50S ribosomal protein 5 beta, chloroplastic"
FT /id="PRO_0000248878"
FT CHAIN 89..142
FT /note="50S ribosomal protein 5 gamma, chloroplastic"
FT /id="PRO_0000248879"
FT REGION 123..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 40..41
FT /note="SF -> TL (in Ref. 3; KNA26006)"
FT /evidence="ECO:0000305"
FT CONFLICT 46..47
FT /note="VA -> MT (in Ref. 3; KNA26006)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="E -> D (in Ref. 3; KNA26006)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="I -> M (in Ref. 3; KNA26006)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..124
FT /note="NRLMRKRK -> TGLCAKES (in Ref. 1; AAA34044)"
FT /evidence="ECO:0000305"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5H1S"
FT HELIX 95..128
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 142 AA; 15621 MW; 87425931C3E4F93F CRC64;
MALLSPLLSL SSVPPITSIA VSSSSFPIKL QNVSVALLPS FGQRLVAHGP VIAQKRGTVV
AMVSAAAEET AGEDGDQSKV EEANISVQNL PLESKLQLKL EQKIKMKMAK KIRLRRNRLM
RKRKLRKRGA WPPSKMKKLK NV
