ID   RS4_ANAMM               Reviewed;         204 AA.
AC   Q5PBD6;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=AM301;
OS   Anaplasma marginale (strain St. Maries).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=234826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=St. Maries;
RX   PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA   Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA   Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT   "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT   is skewed to two superfamilies of outer membrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV86393.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000030; AAV86393.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q5PBD6; -.
DR   SMR; Q5PBD6; -.
DR   KEGG; ama:AM301; -.
DR   HOGENOM; CLU_092403_0_0_5; -.
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..204
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_0000293235"
FT   DOMAIN          93..156
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ   SEQUENCE   204 AA;  22901 MW;  626699BCFA917106 CRC64;
     MVAVVERKYR ASRRLGVNLW GRSKDPVATR NYPSGQHGSM GYKKLSSFGR QFAAHQKFKC
     YYAMSSKQLT NTFLRAYNRK GDTGDNLVGA LESRLAVVVY SAGFVPTVFS ARQLVSHKHV
     TVNGKVVNIP SFSVKPGDVV QIRERATELP MVLAAIQSQE RRVPDHLEVD TAQRSARYLR
     VPKYCEVPYP ANMEVNLVVE FFSG