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Database: UniProt
Entry: A0A1J0A8N6_9ENTE
LinkDB: A0A1J0A8N6_9ENTE
Original site: A0A1J0A8N6_9ENTE 
ID   A0A1J0A8N6_9ENTE        Unreviewed;       115 AA.
AC   A0A1J0A8N6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Large ribosomal subunit protein uL14 {ECO:0000256|HAMAP-Rule:MF_01367};
GN   Name=rplN {ECO:0000256|HAMAP-Rule:MF_01367};
GN   ORFNames=BHY08_10190 {ECO:0000313|EMBL:APB32286.1};
OS   Vagococcus teuberi.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX   NCBI_TaxID=519472 {ECO:0000313|EMBL:APB32286.1, ECO:0000313|Proteomes:UP000191200};
RN   [1] {ECO:0000313|EMBL:APB32286.1, ECO:0000313|Proteomes:UP000191200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21459 {ECO:0000313|EMBL:APB32286.1,
RC   ECO:0000313|Proteomes:UP000191200};
RA   Wullschleger S., Seifert C., Baumgartner S., Lacroix C., Bonfoh B.,
RA   Stevens M.J., Meile L.;
RT   "Vagococcus teuberi sp. nov., isolated from the Malian artisanal sour milk
RT   fene.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit bridges in
CC       the 70S ribosome. {ECO:0000256|HAMAP-Rule:MF_01367,
CC       ECO:0000256|RuleBase:RU003950}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and
CC       together make contacts with the 16S rRNA in bridges B5 and B8.
CC       {ECO:0000256|HAMAP-Rule:MF_01367}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01367, ECO:0000256|RuleBase:RU003949}.
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DR   EMBL; CP017267; APB32286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J0A8N6; -.
DR   STRING; 519472.BHY08_10190; -.
DR   KEGG; vte:BHY08_10190; -.
DR   Proteomes; UP000191200; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.150.20; Ribosomal protein L14; 1.
DR   HAMAP; MF_01367; Ribosomal_L14; 1.
DR   InterPro; IPR000218; Ribosomal_uL14.
DR   InterPro; IPR005745; Ribosomal_uL14_bac-type.
DR   InterPro; IPR019972; Ribosomal_uL14_CS.
DR   InterPro; IPR036853; Ribosomal_uL14_sf.
DR   NCBIfam; TIGR01067; rplN_bact; 1.
DR   PANTHER; PTHR11761; 50S/60S RIBOSOMAL PROTEIN L14/L23; 1.
DR   PANTHER; PTHR11761:SF3; 54S RIBOSOMAL PROTEIN L38, MITOCHONDRIAL; 1.
DR   Pfam; PF00238; Ribosomal_L14; 1.
DR   SMART; SM01374; Ribosomal_L14; 1.
DR   SUPFAM; SSF50193; Ribosomal protein L14; 1.
DR   PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000191200};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01367};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01367};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01367};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01367}.
SQ   SEQUENCE   115 AA;  12298 MW;  6CD3432AF8280504 CRC64;
     MKVADNSGAR EVLTIKVLGG SGRKTANIGD VVVCTVKQAT PGGVVKKGEV VKAVIVRTKS
     GARRSDGSYI KFDENACVII RDDKSPRGTR IFGPVARELR DNNFMKIVSL APEVL
//
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