ID H5X6B0_9PSEU Unreviewed; 139 AA.
AC H5X6B0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=SacmaDRAFT_0699 {ECO:0000313|EMBL:EHR48995.1};
OS Saccharomonospora marina XMU15.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR48995.1, ECO:0000313|Proteomes:UP000004926};
RN [1] {ECO:0000313|EMBL:EHR48995.1, ECO:0000313|Proteomes:UP000004926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR48995.1,
RC ECO:0000313|Proteomes:UP000004926};
RX PubMed=22768369; DOI=10.4056/sigs.2655905;
RA Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT type strain (XMU15(T)).";
RL Stand. Genomic Sci. 6:265-275(2012).
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; CM001439; EHR48995.1; -; Genomic_DNA.
DR RefSeq; WP_009152383.1; NZ_CM001439.1.
DR AlphaFoldDB; H5X6B0; -.
DR STRING; 882083.SacmaDRAFT_0699; -.
DR eggNOG; COG0197; Bacteria.
DR HOGENOM; CLU_078858_2_1_11; -.
DR OrthoDB; 9802589at2; -.
DR Proteomes; UP000004926; 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:UP000004926};
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..25
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 139 AA; 15818 MW; 6B349E56E9AB6869 CRC64;
MLIPRKVKHR KQHSPKRSGA AKGGTKVNFG EYGIQALEHS YVTNRQIESA RIAMTRHIKR
GGKIWINIFP DRPLTKKPAE TRMGSGKGSP EWWVANVKPG RVMFEMSFPN EAVAREALRR
AIHKLPMKCR IVTREGGEF
//