ID   RL9_SHIDS               Reviewed;         149 AA.
AC   Q328J6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503};
GN   Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; OrderedLocusNames=SDY_4372;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00503}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00503}.
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DR   EMBL; CP000034; ABB64259.1; -; Genomic_DNA.
DR   RefSeq; WP_001196060.1; NC_007606.1.
DR   RefSeq; YP_405750.1; NC_007606.1.
DR   AlphaFoldDB; Q328J6; -.
DR   SMR; Q328J6; -.
DR   STRING; 300267.SDY_4372; -.
DR   EnsemblBacteria; ABB64259; ABB64259; SDY_4372.
DR   KEGG; sdy:SDY_4372; -.
DR   PATRIC; fig|300267.13.peg.5161; -.
DR   HOGENOM; CLU_078938_4_1_6; -.
DR   OMA; MKIILTH; -.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; 3.10.430.100; -; 1.
DR   Gene3D; 3.40.5.10; -; 1.
DR   HAMAP; MF_00503; Ribosomal_L9; 1.
DR   InterPro; IPR000244; Ribosomal_L9.
DR   InterPro; IPR009027; Ribosomal_L9/RNase_H1_N.
DR   InterPro; IPR020594; Ribosomal_L9_bac/chp.
DR   InterPro; IPR020069; Ribosomal_L9_C.
DR   InterPro; IPR036791; Ribosomal_L9_C_sf.
DR   InterPro; IPR020070; Ribosomal_L9_N.
DR   InterPro; IPR036935; Ribosomal_L9_N_sf.
DR   PANTHER; PTHR21368; PTHR21368; 1.
DR   Pfam; PF03948; Ribosomal_L9_C; 1.
DR   Pfam; PF01281; Ribosomal_L9_N; 1.
DR   SUPFAM; SSF55653; SSF55653; 1.
DR   SUPFAM; SSF55658; SSF55658; 1.
DR   TIGRFAMs; TIGR00158; L9; 1.
DR   PROSITE; PS00651; RIBOSOMAL_L9; 1.
PE   3: Inferred from homology;
KW   Acetylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..149
FT                   /note="50S ribosomal protein L9"
FT                   /id="PRO_0000236586"
FT   MOD_RES         89
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00503"
SQ   SEQUENCE   149 AA;  15770 MW;  18F2327DB33EFAC2 CRC64;
     MQVILLDKVA NLGSLGDQVN VKAGYARNFL VPQGKAVPAT KKNIEFFEAR RAELEAKLAE
     VLAAANARAE KIDALETVTI ASKAGDEGKL FGSIGTRDIA DAVTAAGVEV AKSEVRLPNG
     VLRTTGEHEV SFQVHSEVFA KVIVNVVAE