ID A0A0J1D3V2_9BURK Unreviewed; 138 AA.
AC A0A0J1D3V2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=EOS_04115 {ECO:0000313|EMBL:KLU27404.1};
OS Caballeronia mineralivorans PML1(12).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU27404.1, ECO:0000313|Proteomes:UP000035963};
RN [1] {ECO:0000313|EMBL:KLU27404.1, ECO:0000313|Proteomes:UP000035963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX PubMed=26205858;
RA Uroz S., Oger P.;
RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT Ability.";
RL Genome Announc. 3:e00798-15(2015).
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:KLU27404.1}.
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DR EMBL; AEJF01000028; KLU27404.1; -; Genomic_DNA.
DR RefSeq; WP_031361576.1; NZ_AEJF01000028.1.
DR AlphaFoldDB; A0A0J1D3V2; -.
DR PATRIC; fig|908627.4.peg.912; -.
DR OrthoDB; 9802589at2; -.
DR Proteomes; UP000035963; 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.
PE 3: Inferred from homology;
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|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01342};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_01342}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 138 AA; 15678 MW; C85AD1BB2A77F64E CRC64;
MLQPKRRKYR KEQKGRNTGK ATRGNAVSFG EYGLKAIGRG RLTARQIEAA RRAMTRHIKR
GGRIWIRIFP DKPISQKPAE VRMGNGKGNP EYYVAEIQPG KMLYEMDGVT EELAREAFRL
AAAKLPLKTY FVSRQLGA
//