ID   RL16_LEPBL              Reviewed;         137 AA.
AC   Q055D7;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=50S ribosomal protein L16 {ECO:0000255|HAMAP-Rule:MF_01342};
GN   Name=rplP1 {ECO:0000255|HAMAP-Rule:MF_01342}; OrderedLocusNames=LBL_0420;
GN   and
GN   Name=rplP2 {ECO:0000255|HAMAP-Rule:MF_01342}; OrderedLocusNames=LBL_0460;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L550;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000348; ABJ78018.1; -; Genomic_DNA.
DR   EMBL; CP000348; ABJ78058.1; -; Genomic_DNA.
DR   RefSeq; WP_011669435.1; NC_008508.1.
DR   AlphaFoldDB; Q055D7; -.
DR   SMR; Q055D7; -.
DR   KEGG; lbl:LBL_0420; -.
DR   KEGG; lbl:LBL_0460; -.
DR   HOGENOM; CLU_078858_2_1_12; -.
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..137
FT                   /note="50S ribosomal protein L16"
FT                   /id="PRO_0000354603"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   137 AA;  15506 MW;  CAF371E7450FE857 CRC64;
     MLSPKRVKFR KRQRGRLKGT DERGSSVSFG EFGLKAVTSG RLTARQIEAA RITINRQVKR
     GGKLWIRIFP HTPITKKPAE TRMGKGKGNP EFWIAEIRPG RILFEMSGID EETAEKALSL
     ASYKLPIHTE FVKRSAL