ID   RL9_ECO8A               Reviewed;         149 AA.
AC   B7M9G5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Large ribosomal subunit protein bL9 {ECO:0000255|HAMAP-Rule:MF_00503};
DE   AltName: Full=50S ribosomal protein L9 {ECO:0000305};
GN   Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; OrderedLocusNames=ECIAI1_4436;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAR01178.1; -; Genomic_DNA.
DR   RefSeq; WP_001196062.1; NC_011741.1.
DR   AlphaFoldDB; B7M9G5; -.
DR   SMR; B7M9G5; -.
DR   GeneID; 83579212; -.
DR   KEGG; ecr:ECIAI1_4436; -.
DR   HOGENOM; CLU_078938_4_1_6; -.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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; Ribosomal protein L9, C-terminal domain; 1.
DR   Gene3D; 3.40.5.10; Ribosomal protein L9, N-terminal domain; 1.
DR   HAMAP; MF_00503; Ribosomal_bL9; 1.
DR   InterPro; IPR000244; Ribosomal_bL9.
DR   InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR   InterPro; IPR020594; Ribosomal_bL9_bac/chp.
DR   InterPro; IPR020069; Ribosomal_bL9_C.
DR   InterPro; IPR036791; Ribosomal_bL9_C_sf.
DR   InterPro; IPR020070; Ribosomal_bL9_N.
DR   InterPro; IPR036935; Ribosomal_bL9_N_sf.
DR   NCBIfam; TIGR00158; L9; 1.
DR   PANTHER; PTHR21368:SF18; 39S RIBOSOMAL PROTEIN L9, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR21368; 50S RIBOSOMAL PROTEIN L9; 1.
DR   Pfam; PF03948; Ribosomal_L9_C; 1.
DR   Pfam; PF01281; Ribosomal_L9_N; 1.
DR   SUPFAM; SSF55658; L9 N-domain-like; 1.
DR   SUPFAM; SSF55653; Ribosomal protein L9 C-domain; 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="Large ribosomal subunit protein bL9"
FT                   /id="PRO_1000126907"
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
//