ID   RL16_STAAB              Reviewed;         144 AA.
AC   Q2YYQ3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=50S ribosomal protein L16 {ECO:0000255|HAMAP-Rule:MF_01342};
GN   Name=rplP {ECO:0000255|HAMAP-Rule:MF_01342}; OrderedLocusNames=SAB2115c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(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}.
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; AJ938182; CAI81804.1; -; Genomic_DNA.
DR   RefSeq; WP_000926310.1; NC_007622.1.
DR   PDB; 6FXC; EM; 6.76 A; AK/BK=1-137.
DR   PDBsum; 6FXC; -.
DR   AlphaFoldDB; Q2YYQ3; -.
DR   SMR; Q2YYQ3; -.
DR   GeneID; 66840455; -.
DR   KEGG; sab:SAB2115c; -.
DR   HOGENOM; CLU_078858_2_1_9; -.
DR   OMA; KGAVEYW; -.
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   1: Evidence at protein level;
KW   3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..144
FT                   /note="50S ribosomal protein L16"
FT                   /id="PRO_0000251674"
FT   REGION          1..23
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   144 AA;  16242 MW;  27B45FD1C2540213 CRC64;
     MLLPKRVKYR RQHRPKTTGR SKGGNYVTFG EFGLQATTTS WITSRQIESA RIAMTRYMKR
     GGKVWIKIFP HTPYTKKPLE VRMGAGKGAV EGWIAVVKPG RILFEVAGVS EEVAREALRL
     ASHKLPVKTK FVKREELGGE TNES