ID   RL9_ECOUT               Reviewed;         149 AA.
AC   Q1R357;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503};
GN   Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; OrderedLocusNames=UTI89_C4803;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE10207.1; -; Genomic_DNA.
DR   RefSeq; WP_001196062.1; NC_007946.1.
DR   AlphaFoldDB; Q1R357; -.
DR   SMR; Q1R357; -.
DR   EnsemblBacteria; ABE10207; ABE10207; UTI89_C4803.
DR   GeneID; 67414822; -.
DR   KEGG; eci:UTI89_C4803; -.
DR   HOGENOM; CLU_078938_4_1_6; -.
DR   OMA; MKIILTH; -.
DR   Proteomes; UP000001952; 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; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..149
FT                   /note="50S ribosomal protein L9"
FT                   /id="PRO_0000258457"
FT   MOD_RES         89
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00503"
SQ   SEQUENCE   149 AA;  15769 MW;  F8FF527DBB9458CA CRC64;
     MQVILLDKVA NLGSLGDQVN VKAGYARNFL VPQGKAVPAT KKNIEFFEAR RAELEAKLAE
     VLAAANARAE KINALETVTI ASKAGDEGKL FGSIGTRDIA DAVTAAGVEV AKSEVRLPNG
     VLRTTGEHEV SFQVHSEVFA KVIVNVVAE