ID   RR4_PELHO               Reviewed;         214 AA.
AC   Q06FV8;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=30S ribosomal protein S4, chloroplastic;
GN   Name=rps4;
OS   Pelargonium hortorum (Common geranium) (Pelargonium inquinans x Pelargonium
OS   zonale).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Geraniales; Geraniaceae; Pelargonium.
OX   NCBI_TaxID=4031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Ringo White;
RX   PubMed=16916942; DOI=10.1093/molbev/msl089;
RA   Chumley T.W., Palmer J.D., Mower J.P., Fourcade H.M., Calie P.J.,
RA   Boore J.L., Jansen R.K.;
RT   "The complete chloroplast genome sequence of Pelargonium x hortorum:
RT   organization and evolution of the largest and most highly rearranged
RT   chloroplast genome of land plants.";
RL   Mol. Biol. Evol. 23:2175-2190(2006).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC       {ECO:0000250}.
CC   -!- FUNCTION: With S5 and S12 plays an important role in translational
CC       accuracy. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC       interaction surface between S4 and S5 is involved in control of
CC       translational fidelity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ897681; ABI17264.1; -; Genomic_DNA.
DR   RefSeq; YP_784073.1; NC_008454.1.
DR   AlphaFoldDB; Q06FV8; -.
DR   SMR; Q06FV8; -.
DR   GeneID; 4362911; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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   3: Inferred from homology;
KW   Chloroplast; Plastid; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..214
FT                   /note="30S ribosomal protein S4, chloroplastic"
FT                   /id="PRO_0000277017"
FT   DOMAIN          92..153
FT                   /note="S4 RNA-binding"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   214 AA;  24893 MW;  8450734DA049460E CRC64;
     MSRYRGPRVK KIKRLGSLPG LTTKKPPIVV RDPRKLSRPK PKKKSQYRIR LEEKQKLRFH
     YGLTERQLLK YVRIAGKAKG PTGQVLLQLL EMRLDNTLFR LGMASTIPQA RQLVNHRHIL
     VNGRIVDIPS YRCKPRDLIS GREKEKSKAL IQNYLDSTAK RPIPLPKHLL LFHSDDPRDL
     LKGSVKKIID RKEVGLKKIK ELLVIEYYSR QISP