ID   RS4_THEAB               Reviewed;         209 AA.
AC   B7IHX2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=THA_1241;
OS   Thermosipho africanus (strain TCF52B).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=484019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCF52B;
RX   PubMed=19124572; DOI=10.1128/jb.01448-08;
RA   Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA   Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT   "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT   the Firmicutes and Archaea.";
RL   J. Bacteriol. 191:1974-1978(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; CP001185; ACJ75686.1; -; Genomic_DNA.
DR   RefSeq; WP_004101494.1; NC_011653.1.
DR   AlphaFoldDB; B7IHX2; -.
DR   SMR; B7IHX2; -.
DR   STRING; 484019.THA_1241; -.
DR   EnsemblBacteria; ACJ75686; ACJ75686; THA_1241.
DR   KEGG; taf:THA_1241; -.
DR   eggNOG; COG0522; Bacteria.
DR   HOGENOM; CLU_092403_0_2_0; -.
DR   OMA; NVVFRMG; -.
DR   OrthoDB; 1211060at2; -.
DR   Proteomes; UP000002453; 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_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; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   PANTHER; PTHR11831; PTHR11831; 1.
DR   PANTHER; PTHR11831:SF4; PTHR11831:SF4; 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; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..209
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_1000140805"
FT   DOMAIN          98..164
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ   SEQUENCE   209 AA;  24502 MW;  614F6BA44CF5CCC0 CRC64;
     MARYTGPQCK LCRREGMKLY LKGERCFTDK CAFDRRPFAP GDHGRDKKKL TQYGIQLRAK
     QTMKRIYGVL ETQFRRYYET ASRKSGDTRE NLVVQVERRL DNVVYRLGFA VNRTTARQLV
     NHGHVLVNGR KVTIPSYQVR PGDVIEIREK SRDILPVKNA IELNKDKNTM PWLTVDYENY
     KGTYERNPKL EEVIDLPVDV QAIIELYSR