ID   RL16_THEFY              Reviewed;         138 AA.
AC   Q47LK0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=50S ribosomal protein L16 {ECO:0000255|HAMAP-Rule:MF_01342};
GN   Name=rplP {ECO:0000255|HAMAP-Rule:MF_01342}; OrderedLocusNames=Tfu_2639;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Binds 23S rRNA and is also seen to make contacts with the A
CC       and possibly P site tRNAs. {ECO:0000255|HAMAP-Rule:MF_01342}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01342}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01342}.
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DR   EMBL; CP000088; AAZ56672.1; -; Genomic_DNA.
DR   RefSeq; WP_011293062.1; NC_007333.1.
DR   AlphaFoldDB; Q47LK0; -.
DR   SMR; Q47LK0; -.
DR   STRING; 269800.Tfu_2639; -.
DR   EnsemblBacteria; AAZ56672; AAZ56672; Tfu_2639.
DR   KEGG; tfu:Tfu_2639; -.
DR   eggNOG; COG0197; Bacteria.
DR   HOGENOM; CLU_078858_2_1_11; -.
DR   OMA; KGAVEYW; -.
DR   OrthoDB; 1786618at2; -.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd01433; Ribosomal_L16_L10e; 1.
DR   Gene3D; 3.90.1170.10; -; 1.
DR   HAMAP; MF_01342; Ribosomal_L16; 1.
DR   InterPro; IPR016180; Ribosomal_L10e/L16.
DR   InterPro; IPR036920; Ribosomal_L10e/L16_sf.
DR   InterPro; IPR000114; Ribosomal_L16.
DR   InterPro; IPR020798; Ribosomal_L16_CS.
DR   PANTHER; PTHR12220; PTHR12220; 1.
DR   Pfam; PF00252; Ribosomal_L16; 1.
DR   PRINTS; PR00060; RIBOSOMALL16.
DR   SUPFAM; SSF54686; SSF54686; 1.
DR   TIGRFAMs; TIGR01164; rplP_bact; 1.
DR   PROSITE; PS00586; RIBOSOMAL_L16_1; 1.
DR   PROSITE; PS00701; RIBOSOMAL_L16_2; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..138
FT                   /note="50S ribosomal protein L16"
FT                   /id="PRO_0000062234"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   138 AA;  15519 MW;  9D26A40F34CCBD39 CRC64;
     MLIPRKVKHR KQHHPSLRGR AKGGTSVHFG EYGIQALESA YVTNRQIEAA RIAMTRHIRR
     GGKVWINIFP DRPLTKKPAE TRMGSGKGSP EWWVAPVKAG RVMFELAGVP EPVAKEALRR
     AIHKLPMKCK VVKREAGE