ID   RS4_THEP1               Reviewed;         209 AA.
AC   A5IMB0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=Tpet_1319;
OS   Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS   RKU-1).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-2007) 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: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; CP000702; ABQ47333.1; -; Genomic_DNA.
DR   RefSeq; WP_011943801.1; NC_009486.1.
DR   AlphaFoldDB; A5IMB0; -.
DR   SMR; A5IMB0; -.
DR   STRING; 390874.Tpet_1319; -.
DR   EnsemblBacteria; ABQ47333; ABQ47333; Tpet_1319.
DR   KEGG; tpt:Tpet_1319; -.
DR   eggNOG; COG0522; Bacteria.
DR   HOGENOM; CLU_092403_0_2_0; -.
DR   OMA; NVVFRMG; -.
DR   Proteomes; UP000006558; 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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..209
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_0000322348"
FT   DOMAIN          98..161
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ   SEQUENCE   209 AA;  24648 MW;  A506E43004692A16 CRC64;
     MARYTGPLCK LCRREGMKLY LKGERCYTDK CAFDRRPYAP GQHGQRRAKL TQYGIQLRAK
     QTVKRIYGIL ERQFERYVEK AMQKAGDTRE NLIQILEARL DNVVYRMGFA INRRQARQLV
     NHGHFLVNGK KVNIPSYLLK PNDVVELREK SRDLEVIKKA VEANKERSVV PWIEVDYDNY
     RGTFLRYPSL EEVTDLPVDL QTVIEFYSR