ID   RS4_DEIRA               Reviewed;         205 AA.
AC   Q9RSJ7;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=DR_2127;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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; AE000513; AAF11677.1; -; Genomic_DNA.
DR   PIR; H75312; H75312.
DR   RefSeq; NP_295850.1; NC_001263.1.
DR   RefSeq; WP_010888758.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RSJ7; -.
DR   SMR; Q9RSJ7; -.
DR   STRING; 243230.DR_2127; -.
DR   EnsemblBacteria; AAF11677; AAF11677; DR_2127.
DR   KEGG; dra:DR_2127; -.
DR   PATRIC; fig|243230.17.peg.2350; -.
DR   eggNOG; COG0522; Bacteria.
DR   HOGENOM; CLU_092403_0_1_0; -.
DR   InParanoid; Q9RSJ7; -.
DR   OMA; NVVFRMG; -.
DR   OrthoDB; 1211060at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..205
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_0000132377"
FT   DOMAIN          95..170
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   205 AA;  23844 MW;  9A6DE63C5C1D9D8F CRC64;
     MGRFRGSITK QSRREGINLA ETEKVQKYLD RRPYGPGQHG QRRKGRPSDY SVRLREKQKL
     ARLYGMNEKQ FRNLFEEASN VPGVTGTVFL QLLERRLDNV VFRMGFASTR RQARQFVGHG
     HILVNGKKVD IASYRVKIGD EISVAEGSRS MGFIQENMDA QKRRRVSPWI EMDQDNFKGT
     FSRLPAREDL ALPINENFII EYYSR