RS3_GLUOX
ID RS3_GLUOX Reviewed; 225 AA.
AC Q5FTY9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; OrderedLocusNames=GOX0374;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW60157.1; -; Genomic_DNA.
DR RefSeq; WP_011251960.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FTY9; -.
DR SMR; Q5FTY9; -.
DR STRING; 290633.GOX0374; -.
DR PRIDE; Q5FTY9; -.
DR EnsemblBacteria; AAW60157; AAW60157; GOX0374.
DR GeneID; 56904640; -.
DR KEGG; gox:GOX0374; -.
DR eggNOG; COG0092; Bacteria.
DR HOGENOM; CLU_058591_0_2_5; -.
DR OMA; KTNPIGN; -.
DR Proteomes; UP000006375; 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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..225
FT /note="30S ribosomal protein S3"
FT /id="PRO_0000130126"
FT DOMAIN 38..106
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
SQ SEQUENCE 225 AA; 25128 MW; 8DA2D84D1B05AD4B CRC64;
MGHKVNPIGL RLGVNRTWDS RWYAGQDYAR LLHEDLKLRA FLRRKLSGAG VSRVVIERPA
KKPRVTIYAA RPGVVIGKKG QDIDALRKEL SRMAKTDVAL NIVEIRKPEI DATLVAENIA
QQLERRVAFR RAMKRAIQSA MRLGAQGIRI TCGGRLGGAE IARAEKYREG RVPLHTLRAD
IDYGTATAKT TYGTCGVKVW IFKGEILAHD PLAQDRRAAE QAPQR