ID   RL6_TROWT               Reviewed;         178 AA.
AC   Q83G00;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365};
GN   Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; OrderedLocusNames=TWT_540;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO44637.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014184; AAO44637.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011096179.1; NC_004572.3.
DR   AlphaFoldDB; Q83G00; -.
DR   SMR; Q83G00; -.
DR   STRING; 203267.TWT_540; -.
DR   EnsemblBacteria; AAO44637; AAO44637; TWT_540.
DR   GeneID; 67387997; -.
DR   KEGG; twh:TWT_540; -.
DR   eggNOG; COG0097; Bacteria.
DR   HOGENOM; CLU_065464_1_2_11; -.
DR   OMA; KPDPYKG; -.
DR   OrthoDB; 1398618at2; -.
DR   Proteomes; UP000002200; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..178
FT                   /note="50S ribosomal protein L6"
FT                   /id="PRO_0000260973"
SQ   SEQUENCE   178 AA;  18817 MW;  C9E4B207F8006C76 CRC64;
     MSRVGKLPIE IPVGVEVCVN GRTVSITGPK GSLYLDIAEQ IGVSVSDGKV LVSRSDDSRT
     ARALHGLTRA LIANNVHGVL HGYTKTLEIV GTGYRVSKKG ENLELALGFS HPVFVDPVPG
     VSFGVEGNSK IIVSGIDKQA VGEAAASIRK LSKPEPYKGK GIRYSDEIVR RKVGKAGK