ID   RS3_THEFY               Reviewed;         270 AA.
AC   Q47LJ9;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN   Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; OrderedLocusNames=Tfu_2640;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ56673.1; -; Genomic_DNA.
DR   RefSeq; WP_011293063.1; NC_007333.1.
DR   AlphaFoldDB; Q47LJ9; -.
DR   SMR; Q47LJ9; -.
DR   STRING; 269800.Tfu_2640; -.
DR   PRIDE; Q47LJ9; -.
DR   EnsemblBacteria; AAZ56673; AAZ56673; Tfu_2640.
DR   KEGG; tfu:Tfu_2640; -.
DR   eggNOG; COG0092; Bacteria.
DR   HOGENOM; CLU_058591_0_2_11; -.
DR   OMA; KTNPIGN; -.
DR   OrthoDB; 1132353at2; -.
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..270
FT                   /note="30S ribosomal protein S3"
FT                   /id="PRO_0000230736"
FT   DOMAIN          38..106
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
FT   REGION          212..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   270 AA;  29949 MW;  7D54E6F827758ED7 CRC64;
     MGQKVNPHGF RLGVTTDFKS RWFADKLYKD YVKEDVAIRQ MLTRGMERAG ISKVEIERTR
     ERVRVDVHTA RPGIVIGRRG AEADRIRANL EKLTNKQVQL NILEVKNPEI DAQLVAQGVA
     EQLSSRVAFR RAMRKAIQSA MKSGAKGIRV QCSGRLGGAE MSRSEFYREG RVPLHTLRAD
     IDYGFFEART TFGRIGVKVW IYKGEAPMTR AEREAAQAAQ RAAGPQRRER PGRRRRGGGG
     GGGQQQQQAE KATAQATEAA KAAKSGNEGS