ID   RL16_ACIF2              Reviewed;         138 AA.
AC   B7J474;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=50S ribosomal protein L16 {ECO:0000255|HAMAP-Rule:MF_01342};
GN   Name=rplP {ECO:0000255|HAMAP-Rule:MF_01342}; OrderedLocusNames=AFE_0334;
OS   Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS   / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=243159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX   PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA   Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA   Eisen J.A., Holmes D.S.;
RT   "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT   industrial applications.";
RL   BMC Genomics 9:597-597(2008).
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; CP001219; ACK79285.1; -; Genomic_DNA.
DR   RefSeq; WP_012536088.1; NC_011761.1.
DR   AlphaFoldDB; B7J474; -.
DR   SMR; B7J474; -.
DR   STRING; 243159.AFE_0334; -.
DR   PaxDb; B7J474; -.
DR   EnsemblBacteria; ACK79285; ACK79285; AFE_0334.
DR   GeneID; 66431390; -.
DR   KEGG; afr:AFE_0334; -.
DR   eggNOG; COG0197; Bacteria.
DR   HOGENOM; CLU_078858_2_1_6; -.
DR   OMA; KGAVEYW; -.
DR   OrthoDB; 1786618at2; -.
DR   Proteomes; UP000001362; 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: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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..138
FT                   /note="50S ribosomal protein L16"
FT                   /id="PRO_1000142912"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   138 AA;  15453 MW;  B1315F49AB2C51CB CRC64;
     MLQPKRTKFR KQHKGRNRGV ATRGSKVSFG EFGLKAVGRG RITARQLEAA RRAISRHVKR
     GGRIWIRIFP DKPISKKPAE VRMGKGKGNP EYWVALIQPG KVLYEMEGVT EEVAREAFAL
     GAAKLPVQTA FVSRRVMG