RS3_LEPBL
ID RS3_LEPBL Reviewed; 225 AA.
AC Q055D8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN Name=rpsC1 {ECO:0000255|HAMAP-Rule:MF_01309}; Synonyms=rpsC-1;
GN OrderedLocusNames=LBL_0419;
GN and
GN Name=rpsC2 {ECO:0000255|HAMAP-Rule:MF_01309}; Synonyms=rpsC;
GN OrderedLocusNames=LBL_0459;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L550;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(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; CP000348; ABJ78017.1; -; Genomic_DNA.
DR EMBL; CP000348; ABJ78057.1; -; Genomic_DNA.
DR RefSeq; WP_002722992.1; NC_008508.1.
DR AlphaFoldDB; Q055D8; -.
DR SMR; Q055D8; -.
DR GeneID; 61172956; -.
DR KEGG; lbl:LBL_0419; -.
DR KEGG; lbl:LBL_0459; -.
DR HOGENOM; CLU_058591_0_2_12; -.
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..225
FT /note="30S ribosomal protein S3"
FT /id="PRO_0000293816"
FT DOMAIN 38..106
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
SQ SEQUENCE 225 AA; 25662 MW; 83FF0BB0712B5879 CRC64;
MGQKVNPIGL RIGITRGWDS IWFSQSDYKK NLHEDIKIRK FIQSRFSNAG VVKVVIERFP
EKINVNLHTA KPGIVIGQKG SNIEAVKKIL KTMTEKPVNL NIIEVKKPET VAQCIAESIA
LQIEQRQPFR RVMKQELRRA MRGGVEGIKI LISGRLNGAD MARRENYKEG RIPLHTLRAK
IDLGFKEAKT TFGQIGVKVW TYSGDFIQSK EESEEDKYAV KRRTS