ID   RS4_EHRCJ               Reviewed;         202 AA.
AC   Q3YSR0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=Ecaj_0194;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jake;
RX   PubMed=16707693; DOI=10.1128/jb.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA   Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA   Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(2006).
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; CP000107; AAZ68245.1; -; Genomic_DNA.
DR   RefSeq; WP_011304323.1; NC_007354.1.
DR   AlphaFoldDB; Q3YSR0; -.
DR   SMR; Q3YSR0; -.
DR   STRING; 269484.Ecaj_0194; -.
DR   EnsemblBacteria; AAZ68245; AAZ68245; Ecaj_0194.
DR   KEGG; ecn:Ecaj_0194; -.
DR   eggNOG; COG0522; Bacteria.
DR   HOGENOM; CLU_092403_0_0_5; -.
DR   OMA; PVICDEQ; -.
DR   OrthoDB; 1211060at2; -.
DR   Proteomes; UP000000435; 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..202
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_0000293272"
FT   DOMAIN          91..168
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ   SEQUENCE   202 AA;  23086 MW;  523F161442D93F56 CRC64;
     MAVQRKYRAS RRLGVSLWGR SKDPFNTRNY PPGQHGNMGY KKPSDFGKQF AAHKKFKFYY
     AISSKQMRNV FLKAYKKRGD TGDNFVGLLE SRLSSILYNS GLVPTIFSAR QLISHKHVLV
     NGKTVNISSY IVKVGDVVTL KEKAKNLPAV IAAIQSQEHK VPDYLEVDTQ EKSVRYLRVP
     KYCEVPYPAT MEVNLVIEFY SR