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Database: UniProt
Entry: A0A291QDE3_9ACTN
LinkDB: A0A291QDE3_9ACTN
Original site: A0A291QDE3_9ACTN 
ID   A0A291QDE3_9ACTN        Unreviewed;       139 AA.
AC   A0A291QDE3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Large ribosomal subunit protein uL16 {ECO:0000256|HAMAP-Rule:MF_01342};
GN   Name=rplP {ECO:0000256|HAMAP-Rule:MF_01342};
GN   ORFNames=KY5_4802 {ECO:0000313|EMBL:ATL29820.1};
OS   Streptomyces formicae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL29820.1, ECO:0000313|Proteomes:UP000221011};
RN   [1] {ECO:0000313|EMBL:ATL29820.1, ECO:0000313|Proteomes:UP000221011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY5 {ECO:0000313|EMBL:ATL29820.1,
RC   ECO:0000313|Proteomes:UP000221011};
RA   Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT   "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT   producer.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds 23S rRNA and is also seen to make contacts with the A
CC       and possibly P site tRNAs. {ECO:0000256|HAMAP-Rule:MF_01342,
CC       ECO:0000256|RuleBase:RU004414}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01342, ECO:0000256|RuleBase:RU004414}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC       {ECO:0000256|ARBA:ARBA00008931, ECO:0000256|HAMAP-Rule:MF_01342,
CC       ECO:0000256|RuleBase:RU004413}.
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DR   EMBL; CP022685; ATL29820.1; -; Genomic_DNA.
DR   RefSeq; WP_055553500.1; NZ_CP022685.1.
DR   AlphaFoldDB; A0A291QDE3; -.
DR   KEGG; sfk:KY5_4802; -.
DR   Proteomes; UP000221011; Chromosome.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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; Ribosomal protein L10e/L16; 1.
DR   HAMAP; MF_01342; Ribosomal_L16; 1.
DR   InterPro; IPR047873; Ribosomal_uL16.
DR   InterPro; IPR000114; Ribosomal_uL16_bact-type.
DR   InterPro; IPR020798; Ribosomal_uL16_CS.
DR   InterPro; IPR016180; Ribosomal_uL16_dom.
DR   InterPro; IPR036920; Ribosomal_uL16_sf.
DR   NCBIfam; TIGR01164; rplP_bact; 1.
DR   PANTHER; PTHR12220:SF13; 39S RIBOSOMAL PROTEIN L16, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12220; 50S/60S RIBOSOMAL PROTEIN L16; 1.
DR   Pfam; PF00252; Ribosomal_L16; 1.
DR   PRINTS; PR00060; RIBOSOMALL16.
DR   SUPFAM; SSF54686; Ribosomal protein L16p/L10e; 1.
DR   PROSITE; PS00586; RIBOSOMAL_L16_1; 1.
DR   PROSITE; PS00701; RIBOSOMAL_L16_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000221011};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01342};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01342};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01342,
KW   ECO:0000256|RuleBase:RU004414};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01342,
KW   ECO:0000256|RuleBase:RU004414};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01342,
KW   ECO:0000256|RuleBase:RU004414}.
FT   REGION          1..24
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   139 AA;  15754 MW;  849F2ED612B0B03E CRC64;
     MLIPRRVKHR KQHHPKRSGM SKGGTQVAFG EYGIQALTPA YVTNRQIEAA RIAMTRHIKR
     GGKVWINIYP DRPLTKKPAE TRMGSGKGSP EWWIANVKPG RVMFELSYPN EKIAREALTR
     AAHKLPMKCK IVKREAGEA
//
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