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RS3_CLOBB
ID   RS3_CLOBB               Reviewed;         221 AA.
AC   B2TII1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN   Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; OrderedLocusNames=CLL_A0244;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in
CC       the 70S ribosome, positioning it for translation. {ECO:0000255|HAMAP-
CC       Rule:MF_01309}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight complex with
CC       proteins S10 and S14. {ECO:0000255|HAMAP-Rule:MF_01309}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01309}.
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DR   EMBL; CP001056; ACD23467.1; -; Genomic_DNA.
DR   RefSeq; WP_012424280.1; NC_018648.1.
DR   AlphaFoldDB; B2TII1; -.
DR   SMR; B2TII1; -.
DR   EnsemblBacteria; ACD23467; ACD23467; CLL_A0244.
DR   KEGG; cbk:CLL_A0244; -.
DR   PATRIC; fig|935198.13.peg.219; -.
DR   HOGENOM; CLU_058591_0_2_9; -.
DR   OMA; KTNPIGN; -.
DR   OrthoDB; 1132353at2; -.
DR   Proteomes; UP000001195; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
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   Gene3D; 3.30.1140.32; -; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   HAMAP; MF_01309_B; Ribosomal_S3_B; 1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR004044; KH_dom_type_2.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR005704; Ribosomal_S3_bac-typ.
DR   InterPro; IPR001351; Ribosomal_S3_C.
DR   InterPro; IPR036419; Ribosomal_S3_C_sf.
DR   InterPro; IPR018280; Ribosomal_S3_CS.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF00189; Ribosomal_S3_C; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54814; SSF54814; 1.
DR   SUPFAM; SSF54821; SSF54821; 1.
DR   TIGRFAMs; TIGR01009; rpsC_bact; 1.
DR   PROSITE; PS50823; KH_TYPE_2; 1.
DR   PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..221
FT                   /note="30S ribosomal protein S3"
FT                   /id="PRO_1000140943"
FT   DOMAIN          39..108
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
SQ   SEQUENCE   221 AA;  24596 MW;  A220B2A1CA03423D CRC64;
     MGQKVHPHGL RVGVIKGWDA KWYANKKDFA DNLVEDNQIR KFVKKELFSA GISKIEIERA
     AKRVKLNIYT AKPGVVIGKG GSGIESLKKK LTNYISGKNI LINIVEVKSV EAEAQLMAEN
     IAAQLEKRIS FRRAMKQTMQ RAMRHGIKGV KTSCSGRLGG AEIARTEHYH EGTIPLQTLR
     ADIDYGFAEA NTTYGKIGVK VWVYKGEVLP TKKVEKEEAN A
 
 
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