ID A0A3P1WGD8_9ACTN Unreviewed; 138 AA.
AC A0A3P1WGD8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=EII42_10765 {ECO:0000313|EMBL:RRD45654.1};
OS Tessaracoccus sp. OH4464_COT-324.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=2491059 {ECO:0000313|EMBL:RRD45654.1, ECO:0000313|Proteomes:UP000274803};
RN [1] {ECO:0000313|EMBL:RRD45654.1, ECO:0000313|Proteomes:UP000274803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH4464_COT-324 {ECO:0000313|EMBL:RRD45654.1,
RC ECO:0000313|Proteomes:UP000274803};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRD45654.1}.
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DR EMBL; RQYZ01000024; RRD45654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1WGD8; -.
DR OrthoDB; 9802589at2; -.
DR Proteomes; UP000274803; Unassembled WGS sequence.
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:UP000274803};
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..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 138 AA; 15620 MW; 91E7190652AEABDC CRC64;
MLIPRRVKFR KQHHPKRDGA AKGGTKLAFG DYGIQALESS YLTNRQIESA RIAMTRHIKR
GGKVWINVYP DRPLTKKPAE TRMGSGKGSP EWWVANVKPG RVLFELSGVA EDVAREAMRL
AIHKLPFKAR FIKREAGE
//