ID   RS4_CHLFF               Reviewed;         209 AA.
AC   Q252M1;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=CF0995;
OS   Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=264202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fe/C-56;
RX   PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA   Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA   Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA   Hattori M., Kuhara S., Shirai M.;
RT   "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL   DNA Res. 13:15-23(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; AP006861; BAE81767.1; -; Genomic_DNA.
DR   RefSeq; WP_011458540.1; NC_007899.1.
DR   AlphaFoldDB; Q252M1; -.
DR   SMR; Q252M1; -.
DR   STRING; 264202.CF0995; -.
DR   KEGG; cfe:CF0995; -.
DR   eggNOG; COG0522; Bacteria.
DR   HOGENOM; CLU_092403_0_1_0; -.
DR   OMA; NVVFRMG; -.
DR   OrthoDB; 1211060at2; -.
DR   Proteomes; UP000001260; 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_0000293257"
FT   DOMAIN          93..156
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT   REGION          23..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   209 AA;  24012 MW;  B5D6BCE435BCDFEC CRC64;
     MARYCGPKNR IARRFGANIF GRSRNPLLKK PHPPGQHGMQ RKKKSDYGLQ LEEKQKLKAC
     YGMILEKQLV KAFKEVVHKQ GSVTKMFLER FECRLDNMVY RMGFAKTIFA AQQLVAHGHV
     LVNGKKVDRR SFFLRPGMQV SLKEKSRKLQ SVQESLENKD ESSLPSYISL DKGNFKGELL
     MSPEQDQMEA QLPLPVDISV VCEFLSHRT