RL9_ECOLU
ID RL9_ECOLU Reviewed; 149 AA.
AC B7NGD7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503};
GN Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; OrderedLocusNames=ECUMN_4736;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
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; CU928163; CAR15849.1; -; Genomic_DNA.
DR RefSeq; WP_001196062.1; NC_011751.1.
DR RefSeq; YP_002415333.1; NC_011751.1.
DR AlphaFoldDB; B7NGD7; -.
DR SMR; B7NGD7; -.
DR STRING; 585056.ECUMN_4736; -.
DR EnsemblBacteria; CAR15849; CAR15849; ECUMN_4736.
DR GeneID; 67414822; -.
DR KEGG; eum:ECUMN_4736; -.
DR PATRIC; fig|585056.7.peg.4899; -.
DR HOGENOM; CLU_078938_4_1_6; -.
DR OMA; MKIILTH; -.
DR Proteomes; UP000007097; 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_1000126909"
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