ID RL9_CORK4 Reviewed; 150 AA.
AC C4LGF9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=ckrop_2080;
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=645127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717;
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
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; CP001620; ACR18778.1; -; Genomic_DNA.
DR RefSeq; WP_012732665.1; NC_012704.1.
DR AlphaFoldDB; C4LGF9; -.
DR SMR; C4LGF9; -.
DR STRING; 645127.ckrop_2080; -.
DR GeneID; 75262613; -.
DR KEGG; ckp:ckrop_2080; -.
DR eggNOG; COG0359; Bacteria.
DR HOGENOM; CLU_078938_5_1_11; -.
DR OrthoDB; 9788336at2; -.
DR Proteomes; UP000001473; Chromosome.
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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..150
FT /note="Large ribosomal subunit protein bL9"
FT /id="PRO_1000206540"
SQ SEQUENCE 150 AA; 16124 MW; 77F00B721D2BE578 CRC64;
MKLILTAAID NLGVPGDIVE VKAGYGRNYL LPRGYAVPAT RGAEKQVQDL KRAQEARAIR
DADRAREVKE QLANLEGVSV AVRTANNGKL FGSVKPNDVA QAVVAAGGPE LDKHSIDMTK
GFVKSTGKYS VDVKLHEDIH GTINFEVVSQ
//