RK31_SPIOL
ID RK31_SPIOL Reviewed; 130 AA.
AC P82249; A0A0K9R0R6; P82246; P82247;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=50S ribosomal protein L31, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=CL31;
DE AltName: Full=Chloroplastic large ribosomal subunit protein bL31c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL31; ORFNames=SOVF_125040;
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 37-60, SUBUNIT, AND SUBCELLULAR LOCATION.
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 -!- MISCELLANEOUS: Three forms, which differ in pI, are produced, L31
CC alpha, L31 beta and L31 gamma. {ECO:0000269|PubMed:10874046}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family.
CC Type A subfamily. {ECO:0000305}.
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DR EMBL; KQ155161; KNA12538.1; -; Genomic_DNA.
DR PDB; 4V61; EM; 9.40 A; 1=42-60.
DR PDB; 5H1S; EM; 3.50 A; a=37-130.
DR PDB; 5MMI; EM; 3.25 A; 0=1-130.
DR PDB; 5MMJ; EM; 3.65 A; 0=1-130.
DR PDB; 5MMM; EM; 3.40 A; 0=1-130.
DR PDB; 5X8P; EM; 3.40 A; 0=37-130.
DR PDB; 5X8T; EM; 3.30 A; 0=37-130.
DR PDB; 6ERI; EM; 3.00 A; AZ=37-102.
DR PDBsum; 4V61; -.
DR PDBsum; 5H1S; -.
DR PDBsum; 5MMI; -.
DR PDBsum; 5MMJ; -.
DR PDBsum; 5MMM; -.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8T; -.
DR PDBsum; 6ERI; -.
DR AlphaFoldDB; P82249; -.
DR SMR; P82249; -.
DR IntAct; P82249; 1.
DR STRING; 3562.P82249; -.
DR OrthoDB; 1618951at2759; -.
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:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 4.10.830.30; -; 1.
DR InterPro; IPR034704; L28p-like.
DR InterPro; IPR002150; Ribosomal_L31.
DR InterPro; IPR042105; Ribosomal_L31_sf.
DR PANTHER; PTHR33280; PTHR33280; 1.
DR Pfam; PF01197; Ribosomal_L31; 1.
DR PRINTS; PR01249; RIBOSOMALL31.
DR SUPFAM; SSF143800; SSF143800; 1.
DR TIGRFAMs; TIGR00105; L31; 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..36
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 37..130
FT /note="50S ribosomal protein L31, chloroplastic"
FT /id="PRO_0000249410"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:5X8T"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:5X8T"
SQ SEQUENCE 130 AA; 14724 MW; 5D423B46829D6935 CRC64;
MVLTLSNQFL AKIPATPKTL TLPKTSSSTL RPQWSCRKSD IHPEFREDAK VYCNGELVMT
TGGTQKDYTV EVWSGNHPFY LGNRSALLLD ADQVEKFRKK YGELTQIMEI PVLKGEIILP
PKKKSKAKKK
