ID   RS4_RHOPB               Reviewed;         205 AA.
AC   Q218M1;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=RPC_1603;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) 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; CP000301; ABD87165.1; -; Genomic_DNA.
DR   RefSeq; WP_011472069.1; NC_007925.1.
DR   AlphaFoldDB; Q218M1; -.
DR   SMR; Q218M1; -.
DR   STRING; 316056.RPC_1603; -.
DR   EnsemblBacteria; ABD87165; ABD87165; RPC_1603.
DR   KEGG; rpc:RPC_1603; -.
DR   eggNOG; COG0522; Bacteria.
DR   HOGENOM; CLU_092403_0_0_5; -.
DR   OMA; NVVFRMG; -.
DR   OrthoDB; 1211060at2; -.
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   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; 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..205
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_0000293353"
FT   DOMAIN          94..157
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT   REGION          18..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   205 AA;  23661 MW;  16E839B5284FEF6D CRC64;
     MTKRSEAKYK IDRRMGQNIW GRPKSPVNRR EYGPGQHGQR RKGKLSDFGV QLRAKQKLKG
     YYANISERQF HSIYVEATRL KGDSGENLIG LLERRLDTVV YRAKFVSTMF AARQFINHGH
     VKVNGKRVNI ASYKVKVGDL VEVKESSKQL TFVLEANQLA ERDVPDFIEV DHGKMTAKFI
     RIPHLSDVPF AVQMEPHLIV EFYSR