ID   RR4_PROWI               Reviewed;         207 AA.
AC   O47032; Q9TJR7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Plastid 30S ribosomal protein S4;
GN   Name=rps4;
OS   Prototheca wickerhamii.
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Prototheca.
OX   NCBI_TaxID=3111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=263-11;
RX   PubMed=12111556; DOI=10.1007/s00438-002-0681-6;
RA   Knauf U., Hachtel W.;
RT   "The genes encoding subunits of ATP synthase are conserved in the reduced
RT   plastid genome of the heterotrophic alga Prototheca wickerhamii.";
RL   Mol. Genet. Genomics 267:492-497(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-207.
RC   STRAIN=263-11;
RA   Knauf U., Wolff G., Kueck U., Hachtel W.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ245645; CAB53104.1; -; Genomic_DNA.
DR   EMBL; AJ222802; CAA10996.1; -; Genomic_DNA.
DR   AlphaFoldDB; O47032; -.
DR   SMR; O47032; -.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
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   Plastid; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..207
FT                   /note="Plastid 30S ribosomal protein S4"
FT                   /id="PRO_0000132657"
FT   DOMAIN          97..158
FT                   /note="S4 RNA-binding"
FT   REGION          20..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        60
FT                   /note="Q -> T (in Ref. 2; CAA10996)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   207 AA;  24058 MW;  932247C37C550198 CRC64;
     MSRYRGPRLP IIRRLGELPG FSKKIDRNHT PPGQHGWKKK ASDQKKSKES QYGIRLKEKQ
     KLRYNYGINE RQLINYVREA RRRKGSTGEV LLQLLEMRLD NIIYRLGFAP TIPAARQLIN
     HGHINVNNKN INIPSYICKI NDIISVLKNS QQLIKNYLQN GGISELSTCL NLNKEKLEAS
     INNIIPRDLV KLEINELLVI EYYSRKL