RR4_SPIOL
ID RR4_SPIOL Reviewed; 201 AA.
AC P13788;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=30S ribosomal protein S4, chloroplastic {ECO:0000303|PubMed:10874039};
DE AltName: Full=Chloroplastic small ribosomal subunit protein uS4c {ECO:0000303|PubMed:28007896};
GN Name=rps4;
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].
RX AGRICOLA=IND87003975; DOI=10.1007/BF00020132;
RA Tahar S.B., Bottomley W., Whitfeld P.R.;
RT "Characterization of the spinach chloroplast genes for the S4 ribosomal
RT protein, tRNA-Thr (UGU) and tRNA-Ser (GGA).";
RL Plant Mol. Biol. 7:63-70(1986).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 2-7, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC STRAIN=cv. Alwaro; TISSUE=Leaf;
RX PubMed=10874039; DOI=10.1074/jbc.m004350200;
RA Yamaguchi K., von Knoblauch K., Subramanian A.R.;
RT "The plastid ribosomal proteins. Identification of all the proteins in the
RT 30S subunit of an organelle ribosome (chloroplast).";
RL J. Biol. Chem. 275:28455-28465(2000).
RN [4]
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 [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 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:10874039,
CC ECO:0000305|PubMed:28007896}.
CC -!- SUBUNIT: Component of the chloroplast small ribosomal subunit (SSU).
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:10874039,
CC ECO:0000269|PubMed:28007896}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10874039, ECO:0000269|PubMed:28007896}.
CC -!- MASS SPECTROMETRY: Mass=23406; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874039};
CC -!- MASS SPECTROMETRY: Mass=23481; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10874039};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
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DR EMBL; AJ400848; CAB88731.1; -; Genomic_DNA.
DR PIR; A30833; A30833.
DR RefSeq; NP_054938.1; NC_002202.1.
DR PDB; 4V61; EM; 9.40 A; AD=1-201.
DR PDB; 5MMJ; EM; 3.65 A; d=1-201.
DR PDB; 5MMM; EM; 3.40 A; d=1-201.
DR PDB; 5X8P; EM; 3.40 A; d=1-201.
DR PDB; 5X8R; EM; 3.70 A; d=1-201.
DR PDB; 6ERI; EM; 3.00 A; BD=2-201.
DR PDBsum; 4V61; -.
DR PDBsum; 5MMJ; -.
DR PDBsum; 5MMM; -.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8R; -.
DR PDBsum; 6ERI; -.
DR AlphaFoldDB; P13788; -.
DR SMR; P13788; -.
DR STRING; 3562.P13788; -.
DR GeneID; 2715646; -.
DR KEGG; soe:2715646; -.
DR OrthoDB; 1507367at2759; -.
DR EvolutionaryTrace; P13788; -.
DR Proteomes; UP000054095; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR005709; Ribosomal_S4_bac-type.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01017; rpsD_bact; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10874039"
FT CHAIN 2..201
FT /note="30S ribosomal protein S4, chloroplastic"
FT /id="PRO_0000132668"
FT DOMAIN 89..149
FT /note="S4 RNA-binding"
FT REGION 15..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 23410 MW; 0685C898ACB2BCCE CRC64;
MSRYRGPRFK KIRRLGALPG LTNKRPRAGS DLRNQSRSGK RSQYRIRLEE KQKLRFHYGI
TERQLLKYVR IARKAKGSTG QVLLQLLEMR LDNILFRLGM APTIPGARQL VNHRHILVNG
RIVDIPSYRC KPQDTIMARD EQKSIALIQN SLDLSPREEL PKHLTLNPFP YKGLVNQIID
SKWVGLKINE LLVVEYYSRQ T
