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RL6_SALTO
ID   RL6_SALTO               Reviewed;         180 AA.
AC   A4XBN1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365};
GN   Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; OrderedLocusNames=Strop_3908;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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; CP000667; ABP56338.1; -; Genomic_DNA.
DR   RefSeq; WP_012015113.1; NC_009380.1.
DR   AlphaFoldDB; A4XBN1; -.
DR   SMR; A4XBN1; -.
DR   STRING; 369723.Strop_3908; -.
DR   EnsemblBacteria; ABP56338; ABP56338; Strop_3908.
DR   KEGG; stp:Strop_3908; -.
DR   PATRIC; fig|369723.5.peg.4034; -.
DR   eggNOG; COG0097; Bacteria.
DR   HOGENOM; CLU_065464_1_2_11; -.
DR   OMA; KPDPYKG; -.
DR   Proteomes; UP000000235; 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..180
FT                   /note="50S ribosomal protein L6"
FT                   /id="PRO_1000087063"
SQ   SEQUENCE   180 AA;  19331 MW;  F4AA55D13794942A CRC64;
     MSRIGRKSIP VPTGVDVTIA GQTVTVKGPK GELSHTIAEP ITIDRAEDGQ LNVARPNDER
     KAKELHGLSR TLVANMIVGV TEGYRKSLEI AGTGYRVTAK GKDLEFALGF SHPVTVVAPE
     GITFSVEKPT LFHVAGINKQ LVGEVAANIR KIRPPEPYKG KGVKYQGEVI RRKAGKAGKK
 
 
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