RS3_BORA1
ID RS3_BORA1 Reviewed; 264 AA.
AC Q2L2C0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; OrderedLocusNames=BAV0031;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ47615.1; -; Genomic_DNA.
DR RefSeq; WP_012415738.1; NC_010645.1.
DR AlphaFoldDB; Q2L2C0; -.
DR SMR; Q2L2C0; -.
DR STRING; 360910.BAV0031; -.
DR EnsemblBacteria; CAJ47615; CAJ47615; BAV0031.
DR GeneID; 41391960; -.
DR KEGG; bav:BAV0031; -.
DR eggNOG; COG0092; Bacteria.
DR HOGENOM; CLU_058591_0_2_4; -.
DR OMA; KTNPIGN; -.
DR OrthoDB; 1132353at2; -.
DR Proteomes; UP000001977; 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..264
FT /note="30S ribosomal protein S3"
FT /id="PRO_0000293758"
FT DOMAIN 39..107
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
FT REGION 214..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 264 AA; 29503 MW; BE9F9C6127B3FBEE CRC64;
MGQKIHPTGF RLAVTRNWSS RWYADDKDFG GMLAEDIRVR EYLKKKLKSA SVGRVVIERP
AKNARITVYS ARPGVVIGKR GEDIESLKAD LQRLMGVPVH VNIEEIRKPE TDAQLIADSI
SQQLEKRIMF RRAMKRAMQN AMRLGAQGIK IMSSGRLNGI EIARTEWYRE GRVPLHTLKA
NIDYGTSEAH TTYGVIGIKV WVYKGDMLAN GELPVETAAP REEERRPRRA PRGDRPDGAR
NGRPGGGRGR APRKADAAPA PEGE
