RK2_SPIOL
ID RK2_SPIOL Reviewed; 272 AA.
AC P06509; Q9M3I1; Q9THV0;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=50S ribosomal protein L2, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL2c {ECO:0000303|PubMed:28007896};
DE AltName: Full=Ribosomal protein CS-L4;
GN Name=rpl2-A;
GN and
GN Name=rpl2-B;
OS Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RX PubMed=6089120; DOI=10.1093/nar/12.16.6547;
RA Zurawski G., Bottomley W., Whitfeld P.R.;
RT "Junctions of the large single copy region and the inverted repeats in
RT Spinacia oleracea and Nicotiana debneyi chloroplast DNA: sequence of the
RT genes for tRNAHis and the ribosomal proteins S19 and L2.";
RL Nucleic Acids Res. 12:6547-6558(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, SUBUNIT, AND
RP 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=3362671; DOI=10.1093/nar/16.6.2461;
RA Thomas F., Massenet O., Dorne A.-M., Briat J.-F., Mache R.;
RT "Expression of the rpl23, rpl2 and rps19 genes in spinach chloroplasts.";
RL Nucleic Acids Res. 16:2461-2472(1988).
RN [5]
RP METHYLATION AT ALA-2, AND PROTEIN SEQUENCE OF 2-14; 123-128; 132-136 AND
RP 222-229.
RC STRAIN=cv. Alwaro;
RA Kamp R.M., Srinivasa B.R., von Knoblauch K., Subramanian A.R.;
RT "Occurrence of a methylated protein in chloroplast ribosomes.";
RL Biochemistry 26:5866-5870(1987).
RN [6]
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 [7]
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 [8]
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 -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000305}.
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DR EMBL; AJ244023; CAB56543.3; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88803.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88768.1; -; Genomic_DNA.
DR EMBL; X07462; CAA30345.1; -; Genomic_DNA.
DR PIR; S07918; R5SP2.
DR RefSeq; NP_055005.1; NC_002202.1.
DR PDB; 4V61; EM; 9.40 A; BE=1-269.
DR PDB; 5H1S; EM; 3.50 A; E=2-272.
DR PDB; 5MLC; EM; 3.90 A; D=1-272.
DR PDB; 5MMI; EM; 3.25 A; C=1-272.
DR PDB; 5MMM; EM; 3.40 A; C=1-272.
DR PDB; 5X8P; EM; 3.40 A; C=2-272.
DR PDB; 5X8T; EM; 3.30 A; C=2-272.
DR PDB; 6ERI; EM; 3.00 A; AC=26-271.
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; P06509; -.
DR SMR; P06509; -.
DR IntAct; P06509; 1.
DR STRING; 3562.P06509; -.
DR GeneID; 2715624; -.
DR KEGG; soe:2715624; -.
DR OrthoDB; 1156335at2759; -.
DR EvolutionaryTrace; P06509; -.
DR Proteomes; UP000054095; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR01171; rplB_bact; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Methylation; Plastid;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10874046,
FT ECO:0000269|PubMed:6089120, ECO:0000269|Ref.5"
FT CHAIN 2..272
FT /note="50S ribosomal protein L2, chloroplastic"
FT /id="PRO_0000129707"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-methylalanine"
FT /evidence="ECO:0000269|Ref.5"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:5H1S"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5H1S"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5H1S"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:5X8T"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 272 AA; 29792 MW; 30D99EF32A743B75 CRC64;
MAIHLYKTST SSTRNGAVQV KSNPRNNLIS GQRRCGKGRN ARGIITARHR GGGHKRLYRK
IDFRRNEKDI YGKIVTIEYD PNRNAYICLI HYGDGEKRYI LHPRGAIIGD TIVSGTEVPI
KMGNALPLTD MPLGTAIHNI EITLGRGGQL ARAAGAVAKL IAKEGKSATL KLPSGEVRLI
SKNCSATVGQ VGNVGVNQKR LGRAGSKRWL GKRPVVRGVV MNPVDHPHGG GEGRAPIGRK
SPTTPWGYPA LGRRSRKRNK YSDNFIIRRR SK
