ID   RS3_BURM9               Reviewed;         266 AA.
AC   A2S7I2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN   Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309};
GN   OrderedLocusNames=BMA10229_A1930;
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000546; ABN00762.1; -; Genomic_DNA.
DR   RefSeq; WP_004185240.1; NC_008836.1.
DR   AlphaFoldDB; A2S7I2; -.
DR   SMR; A2S7I2; -.
DR   EnsemblBacteria; ABN00762; ABN00762; BMA10229_A1930.
DR   GeneID; 56594549; -.
DR   KEGG; bml:BMA10229_A1930; -.
DR   HOGENOM; CLU_058591_0_2_4; -.
DR   OMA; KTNPIGN; -.
DR   Proteomes; UP000002283; Chromosome I.
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..266
FT                   /note="30S ribosomal protein S3"
FT                   /id="PRO_1000086097"
FT   DOMAIN          39..107
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
FT   REGION          214..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   266 AA;  29919 MW;  92B4A519A53E7D23 CRC64;
     MGQKIHPTGF RLAVSRNWAS RWYANNNNFA AMLQEDIGVR EYLKKKLKNA SVGRVVIERP
     AKNARITIFS SRPGVVIGKK GEDIELLKTE LQRRMGVPVH VNIEEIRKPE TDAQLIADSI
     TQQLERRIMF RRAMKRAMQN AMRLGAQGIK IMSAGRLNGI EIARTEWYRE GRVPLHTLRA
     DIDYATSEAK TTYGIIGVKV WVYKGDTLGR NDAPVVEEVT EDKRPRRNAR PGDRRPRRDG
     EGGAPGARRG GPRRGAGKPE DGKTGE