ID   RS3_PORGI               Reviewed;         246 AA.
AC   Q7MTL9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN   Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; OrderedLocusNames=PG_1932;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ66913.1; -; Genomic_DNA.
DR   RefSeq; WP_004583592.1; NC_002950.2.
DR   AlphaFoldDB; Q7MTL9; -.
DR   SMR; Q7MTL9; -.
DR   STRING; 242619.PG_1932; -.
DR   EnsemblBacteria; AAQ66913; AAQ66913; PG_1932.
DR   GeneID; 57239590; -.
DR   KEGG; pgi:PG_1932; -.
DR   eggNOG; COG0092; Bacteria.
DR   HOGENOM; CLU_058591_0_2_10; -.
DR   OMA; KTNPIGN; -.
DR   OrthoDB; 1132353at2; -.
DR   Proteomes; UP000000588; 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..246
FT                   /note="30S ribosomal protein S3"
FT                   /id="PRO_0000130173"
FT   DOMAIN          38..106
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
FT   REGION          218..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   246 AA;  27570 MW;  E117C31DF4A0B685 CRC64;
     MGQKINPVSN RLGIIRGWDS NWYGGRKYGE TLLEDSRIRQ YLNARLAKAS VSRIVIERAL
     KLVTITICTA RPGMIIGKAG QEVDKLKEEL KRITKKDVQI NIYEIRKPEL DAAIVAENIA
     RQLEGKIAYR RAVKMAIASA MRMGAEGIKI QVSGRLNGAE MARSEMFKEG RTPLHTLRAD
     IDYALAEALT KVGLLGIKVW ICKGEVYEKR DLAPNFAVAK NQSRRPNAQG GNNRGGDRNR
     RRKGNR