ID A0A1A0FH82_9GAMM Unreviewed; 137 AA.
AC A0A1A0FH82;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=ADS46_15020 {ECO:0000313|EMBL:OAZ98782.1};
OS Halomonas sp. G11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1684425 {ECO:0000313|EMBL:OAZ98782.1, ECO:0000313|Proteomes:UP000092250};
RN [1] {ECO:0000313|EMBL:OAZ98782.1, ECO:0000313|Proteomes:UP000092250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G11 {ECO:0000313|EMBL:OAZ98782.1,
RC ECO:0000313|Proteomes:UP000092250};
RA Naifar M., Chouchane H., Najjari A., El Hidri D., Mahjoubi M., Ghedira K.,
RA Soufi L., Salah A., Raddadi N., Sghaier H., Ouzari H.I.,
RA Eddine Masmoudi A.S., Cherif A.;
RT "Genomic basis for crude oil degradation, heavy metal resistance and high
RT salt tolerance of Halomonas hydrocarbonoclasticus G11 isolated from
RT Tunisian Chott El-Djerid salt lake.";
RL Submitted (FEB-2016) 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:OAZ98782.1}.
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DR EMBL; LYXG01000014; OAZ98782.1; -; Genomic_DNA.
DR RefSeq; WP_066318565.1; NZ_LYXG01000014.1.
DR AlphaFoldDB; A0A1A0FH82; -.
DR OrthoDB; 9802589at2; -.
DR Proteomes; UP000092250; 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 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..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 137 AA; 15606 MW; D15E31BA2284785B CRC64;
MLQPKRMKFR KMQKGRNRGL AHRGSKISFG EYGLKATGRG RVTARQIEAG RRAITRHVKR
GGKIWIRVFP DKPISKKPLE VRMGKGKGSV EYWVAQIQPG RVLYEIEGVP EELAREAFEL
AAQKMPISTT FAKRTVM
//
