ID E7G4J8_9HELI Unreviewed; 141 AA.
AC E7G4J8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Large ribosomal subunit protein uL16 {ECO:0000256|HAMAP-Rule:MF_01342};
GN Name=rplP {ECO:0000256|HAMAP-Rule:MF_01342,
GN ECO:0000313|EMBL:EFX41691.1};
GN ORFNames=HSUHS5_0909 {ECO:0000313|EMBL:EFX41691.1};
OS Helicobacter suis HS5.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=710394 {ECO:0000313|EMBL:EFX41691.1, ECO:0000313|Proteomes:UP000054093};
RN [1] {ECO:0000313|EMBL:EFX41691.1, ECO:0000313|Proteomes:UP000054093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS5 {ECO:0000313|EMBL:EFX41691.1,
RC ECO:0000313|Proteomes:UP000054093};
RX PubMed=21414191; DOI=10.1186/1297-9716-42-51;
RA Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A.,
RA De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.;
RT "Genome sequence of Helicobacter suis supports its role in gastric
RT pathology.";
RL Vet. Res. 42:51-51(2011).
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:EFX41691.1}.
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DR EMBL; ADHO01000173; EFX41691.1; -; Genomic_DNA.
DR RefSeq; WP_006565271.1; NZ_ADHO01000173.1.
DR AlphaFoldDB; E7G4J8; -.
DR GeneID; 56927927; -.
DR Proteomes; UP000054093; 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:UP000054093};
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 141 AA; 16109 MW; 15EB810CAF1AF653 CRC64;
MLMPKKTKYR KQMKGRNRGK STRGASLAFG DVGIKAVEHG RIDSRQIEAA RVAMTRHTKR
TGKVWIRVFP DKPLTAKPLE TRMGKGKGSV EKWVMNIKPG RIIYEMLGIE EEVAREALAL
AQRKLPFKTK IVTRESENEI Y
//
