ID   RS4B_CLOB1              Reviewed;         197 AA.
AC   A7FZ00;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=30S ribosomal protein S4 B {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rpsD2 {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=CLB_3462;
OS   Clostridium botulinum (strain ATCC 19397 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19397 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000726; ABS34917.1; -; Genomic_DNA.
DR   RefSeq; WP_003401493.1; NC_009697.1.
DR   AlphaFoldDB; A7FZ00; -.
DR   SMR; A7FZ00; -.
DR   GeneID; 5187000; -.
DR   KEGG; cba:CLB_3462; -.
DR   HOGENOM; CLU_092403_0_1_9; -.
DR   OMA; PVICDEQ; -.
DR   OrthoDB; 1211060at2; -.
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..197
FT                   /note="30S ribosomal protein S4 B"
FT                   /id="PRO_0000322286"
FT   DOMAIN          88..151
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ   SEQUENCE   197 AA;  23036 MW;  5FE652DC6C400AE1 CRC64;
     MAKIRDPRFK LSRRLGVNIY GHPKAMKRAT RENSREGKKL SNYGKQLLEK QKIRSYYGVL
     EKQFLRYVKK AMKSKERTGD VLLRSLECRL DNIAYRIGFA NSIRQARQMV NHGHILVNGS
     KVNIPSYEVK TGDVITLREK YRKNDEFADN FLALKKFSLP YIEKDYDKFS GVLIKEPERD
     EIPIDANETL VVELYSK