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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
 
 
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