RS3_HERAR
ID RS3_HERAR Reviewed; 283 AA.
AC A4G9T2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; OrderedLocusNames=HEAR3160;
OS Herminiimonas arsenicoxydans.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1;
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.-C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(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; CU207211; CAL63269.1; -; Genomic_DNA.
DR RefSeq; WP_011872523.1; NC_009138.1.
DR AlphaFoldDB; A4G9T2; -.
DR SMR; A4G9T2; -.
DR STRING; 204773.HEAR3160; -.
DR PRIDE; A4G9T2; -.
DR EnsemblBacteria; CAL63269; CAL63269; HEAR3160.
DR KEGG; har:HEAR3160; -.
DR eggNOG; COG0092; Bacteria.
DR HOGENOM; CLU_058591_0_2_4; -.
DR OMA; KTNPIGN; -.
DR OrthoDB; 1132353at2; -.
DR Proteomes; UP000006697; 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..283
FT /note="30S ribosomal protein S3"
FT /id="PRO_1000086127"
FT DOMAIN 39..107
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
FT REGION 209..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 283 AA; 31234 MW; 3E9993DD4844EEF5 CRC64;
MGQKIHPTGF RLSVTRNWAS RWYAGNSNFA TMLNEDLKVR AYLKTKLKNA SVGRVIIERP
AKNARITIYS SRPGVVIGKK GEDIEVLKSA LTKMMGVPVH VNIEEIRKPE TDAQLIADSI
AQQLEKRIMF RRAMKRAMQN AMRLGAQGIK IMSSGRLNGI EIARKEWYRE GRVPLHTLRA
EIDYGFGEAE TTYGIIGIKV WVYKGDRLPS GEPPVDLTKE DDTKRRGPRR DDGKPSSRPR
TARPEGQPGA AAAPGAAPAA KRVRAKKPDA AVDGAVPAEK AGE