ID   RL6_MICLU               Reviewed;         178 AA.
AC   P33099;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
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};
OS   Micrococcus luteus (Micrococcus lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=1270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2533272; DOI=10.1007/bf02602908;
RA   Ohama T., Muto A., Osawa S.;
RT   "Spectinomycin operon of Micrococcus luteus: evolutionary implications of
RT   organization and novel codon usage.";
RL   J. Mol. Evol. 29:381-395(1989).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X17524; CAA35562.1; -; Genomic_DNA.
DR   PIR; S29886; S29886.
DR   AlphaFoldDB; P33099; -.
DR   SMR; P33099; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..178
FT                   /note="50S ribosomal protein L6"
FT                   /id="PRO_0000131056"
SQ   SEQUENCE   178 AA;  19255 MW;  98DDB37A7D40BA45 CRC64;
     MSRIGRLPIT IPAGVDVTID GDRVSVKGPK GPKGQLEHSL PTPITATLEE GQVTVARPDD
     ERESRSLHGL TRTLISNMVE GVTNGFSKQL EVVGTGYRVQ AKGQDLEFDL GYSHPVPVKV
     SQGITFTVEG NRVTVAGIDK QQQVGETAAN IRKLRRPDPY KGKGVYAGEQ IRRKAGKK