ID   RR4_PHAAO               Reviewed;         201 AA.
AC   Q3BAN8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=30S ribosomal protein S4, chloroplastic;
GN   Name=rps4;
OS   Phalaenopsis aphrodite subsp. formosana (Moth orchid).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Vandeae; Aeridinae; Phalaenopsis.
OX   NCBI_TaxID=308872;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Taisugar TS-97;
RX   PubMed=16207935; DOI=10.1093/molbev/msj029;
RA   Chang C.-C., Lin H.-C., Lin I.-P., Chow T.-Y., Chen H.-H., Chen W.-H.,
RA   Cheng C.-H., Lin C.-Y., Liu S.-M., Chang C.-C., Chaw S.-M.;
RT   "The chloroplast genome of Phalaenopsis aphrodite (Orchidaceae):
RT   comparative analysis of evolutionary rate with that of grasses and its
RT   phylogenetic implications.";
RL   Mol. Biol. Evol. 23:279-291(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}.
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DR   EMBL; AY916449; AAW82505.1; -; Genomic_DNA.
DR   RefSeq; YP_358580.1; NC_007499.1.
DR   AlphaFoldDB; Q3BAN8; -.
DR   SMR; Q3BAN8; -.
DR   GeneID; 3741679; -.
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..201
FT                   /note="30S ribosomal protein S4, chloroplastic"
FT                   /id="PRO_0000228953"
FT   DOMAIN          89..150
FT                   /note="S4 RNA-binding"
SQ   SEQUENCE   201 AA;  23439 MW;  76F7BC12C21090DC CRC64;
     MSRYRGPRFK KIRRLGVLPG LTSKRPRSRS DLQTQLRFGK RSQYRIRLEE KQKLRFHYGL
     TERQLLKYVH IAGKAKGSTG QVLLQLLEMR LDNILFRLGM ASTIPGARQL VNHRHILVNG
     RIVDIPSYRC KPLDIITTKD KERSKALIQN YLVSSPRGEL PNHLTIDSLQ YKGFVNQIID
     SKWIGLKINE LLVVEYYSRQ T