ID   RS4_SULIL               Reviewed;         181 AA.
AC   C3MJP5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rps4 {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=LS215_2211;
OS   Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=429572;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.S.2.15 / Lassen #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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:0000255|HAMAP-Rule:MF_01306}.
CC   -!- FUNCTION: With S5 and S12 plays an important role in translational
CC       accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}.
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. {ECO:0000255|HAMAP-Rule:MF_01306}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01306}.
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DR   EMBL; CP001399; ACP36198.1; -; Genomic_DNA.
DR   RefSeq; WP_012712013.1; NC_012589.1.
DR   AlphaFoldDB; C3MJP5; -.
DR   SMR; C3MJP5; -.
DR   EnsemblBacteria; ACP36198; ACP36198; LS215_2211.
DR   GeneID; 7811943; -.
DR   GeneID; 7939381; -.
DR   GeneID; 8762163; -.
DR   KEGG; sis:LS215_2211; -.
DR   HOGENOM; CLU_089738_1_1_2; -.
DR   OMA; ARQFITH; -.
DR   OrthoDB; 93256at2157; -.
DR   Proteomes; UP000001747; Chromosome.
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_A; Ribosomal_S4_A; 1.
DR   InterPro; IPR022801; Ribosomal_S4/S9.
DR   InterPro; IPR005710; Ribosomal_S4/S9_euk/arc.
DR   InterPro; IPR001912; Ribosomal_S4/S9_N.
DR   InterPro; IPR022802; Ribosomal_S4_arc.
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; PF01479; S4; 1.
DR   SMART; SM01390; Ribosomal_S4; 1.
DR   SMART; SM00363; S4; 1.
DR   TIGRFAMs; TIGR01018; uS4_arch; 1.
DR   PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..181
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_1000214305"
FT   DOMAIN          104..166
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ   SEQUENCE   181 AA;  20688 MW;  F128638F2C7A7E3F CRC64;
     MGDPKKSRKK WESPGHPWIK ERIGYEQELL GKYGLRNKRE IWIAQSIIRK FRHQARSLLA
     LPPAERAVRE KQLVGKLLKM GLLKRETATV DDILSLTEQD LLERRLQTIV YKKGLANTTY
     QARQLIIHGH IAVNGKRVTS PGYIVNVDEE NLIDYYVTSS FKSRPPVMAQ QEGGEAGVKQ
     A