ID   RL6_CAUVN               Reviewed;         177 AA.
AC   B8H4E9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365};
GN   Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; OrderedLocusNames=CCNA_01321;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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; CP001340; ACL94786.1; -; Genomic_DNA.
DR   RefSeq; WP_010919142.1; NC_011916.1.
DR   RefSeq; YP_002516694.1; NC_011916.1.
DR   AlphaFoldDB; B8H4E9; -.
DR   SMR; B8H4E9; -.
DR   PRIDE; B8H4E9; -.
DR   EnsemblBacteria; ACL94786; ACL94786; CCNA_01321.
DR   GeneID; 7333053; -.
DR   KEGG; ccs:CCNA_01321; -.
DR   PATRIC; fig|565050.3.peg.1305; -.
DR   HOGENOM; CLU_065464_1_2_5; -.
DR   OMA; KPDPYKG; -.
DR   OrthoDB; 1398618at2; -.
DR   PhylomeDB; B8H4E9; -.
DR   Proteomes; UP000001364; 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..177
FT                   /note="50S ribosomal protein L6"
FT                   /id="PRO_1000166796"
FT   REGION          157..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   177 AA;  18885 MW;  DE2FE5DC3057F367 CRC64;
     MSRIGKKAVA IPSGVQVTLA GQTVTVKGPK GQLSWTIADE VEVKQEGAEL LLAPRVDTKR
     AKGMWGLSRT LVANMVHGVT VGFEESLELV GVGYRAAMKG TALSLQLGFS HDVDVAAPAG
     VTFAVPKQTE IKIAGIDKQA VGEIAAKIRR IRPPEPYKGK GVRYAGEKVR RKEGKKK