ID   RS4_BORAP               Reviewed;         208 AA.
AC   Q0SMP1; G0IQG5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306};
GN   OrderedLocusNames=BAPKO_0652, BafPKo_0635;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH01887.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69835.1; -; Genomic_DNA.
DR   RefSeq; WP_011601126.1; NC_008277.1.
DR   AlphaFoldDB; Q0SMP1; -.
DR   SMR; Q0SMP1; -.
DR   STRING; 390236.BafPKo_0635; -.
DR   EnsemblBacteria; AEL69835; AEL69835; BafPKo_0635.
DR   KEGG; baf:BAPKO_0652; -.
DR   KEGG; bafz:BafPKo_0635; -.
DR   PATRIC; fig|390236.22.peg.608; -.
DR   eggNOG; COG0522; Bacteria.
DR   HOGENOM; CLU_092403_0_4_12; -.
DR   OMA; NVVFRMG; -.
DR   Proteomes; UP000005216; 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..208
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_0000293248"
FT   DOMAIN          95..159
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT   CONFLICT        72
FT                   /note="P -> T (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="Y -> D (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95..96
FT                   /note="TI -> RR (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="F -> I (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="L -> Q (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143..147
FT                   /note="LIQEI -> QIKEK (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="G -> R (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        160
FT                   /note="Q -> K (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163..164
FT                   /note="AQ -> SL (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="G -> W (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173
FT                   /note="L -> V (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="Y -> D (in Ref. 2; AEL69835)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   208 AA;  23721 MW;  E3B7AFE24964256E CRC64;
     MNRKQIAKGK LVRRFGINIF EQPKYDKILK KKPHPPGMHG KARKAKITEY GKQLIEKQKI
     KFTYGVSERQ LPNTFKEAKK HHGVTGYNLL SILETIIDNI VYRAGFAFSR AHARLIVSHG
     IVILNGRRVT IPSIILRAND QILIQEIDSL KKLIGSNIEQ TSAQRNLPTG IELNADYLNI
     KVKHAPSRDE IPTLANEQMV VEYYSKRA