ID   RL6_YERPA               Reviewed;         177 AA.
AC   Q1C2W2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365};
GN   Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; OrderedLocusNames=YPA_3248;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: This protein binds to the 23S rRNA, and is important in its
CC       secondary structure. It is located near the subunit interface in the
CC       base of the L7/L12 stalk, and near the tRNA binding site of the
CC       peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01365}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01365}.
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DR   EMBL; CP000308; ABG15210.1; -; Genomic_DNA.
DR   RefSeq; WP_002213334.1; NZ_CP009906.1.
DR   AlphaFoldDB; Q1C2W2; -.
DR   SMR; Q1C2W2; -.
DR   EnsemblBacteria; ABG15210; ABG15210; YPA_3248.
DR   GeneID; 66843893; -.
DR   KEGG; ypa:YPA_3248; -.
DR   OMA; KPDPYKG; -.
DR   Proteomes; UP000001971; 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; 3.90.930.12; -; 2.
DR   HAMAP; MF_01365_B; Ribosomal_L6_B; 1.
DR   InterPro; IPR000702; Ribosomal_L6.
DR   InterPro; IPR020040; Ribosomal_L6_a/b-dom.
DR   InterPro; IPR036789; Ribosomal_L6_a/b-dom_sf.
DR   InterPro; IPR019906; Ribosomal_L6_bac-type.
DR   InterPro; IPR002358; Ribosomal_L6_CS.
DR   PANTHER; PTHR11655; PTHR11655; 1.
DR   PANTHER; PTHR11655:SF14; PTHR11655:SF14; 1.
DR   Pfam; PF00347; Ribosomal_L6; 2.
DR   PIRSF; PIRSF002162; Ribosomal_L6; 1.
DR   PRINTS; PR00059; RIBOSOMALL6.
DR   SUPFAM; SSF56053; SSF56053; 2.
DR   TIGRFAMs; TIGR03654; L6_bact; 1.
DR   PROSITE; PS00525; RIBOSOMAL_L6_1; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..177
FT                   /note="50S ribosomal protein L6"
FT                   /id="PRO_0000265314"
SQ   SEQUENCE   177 AA;  18927 MW;  2CDF5DF6EC5D1062 CRC64;
     MSRVAKAPVV IPAGVEVKLN GQVISIKGKN GELTRTVHSA VEVKQEENTL TFAPREGAVD
     GWAQAGTTRA LLNSMVIGVT EGFTKKLQLV GVGYRAAVKG NVVNLALGFS HPVDHELPAG
     ITAECPTQTE IVLKGADKQV IGQVAADLRA YRRPEPYKGK GVRYADEVVR TKEAKKK