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Database: UniProt
Entry: T2KJW3_FORAG
LinkDB: T2KJW3_FORAG
Original site: T2KJW3_FORAG 
ID   T2KJW3_FORAG            Unreviewed;       122 AA.
AC   T2KJW3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=BN863_5720 {ECO:0000313|EMBL:CDF78284.1};
OS   Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS   M-2Alg 35-1).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Formosa.
OX   NCBI_TaxID=1347342 {ECO:0000313|EMBL:CDF78284.1, ECO:0000313|Proteomes:UP000016160};
RN   [1] {ECO:0000313|EMBL:CDF78284.1, ECO:0000313|Proteomes:UP000016160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901
RC   {ECO:0000313|Proteomes:UP000016160};
RX   PubMed=23995932; DOI=10.1128/AEM.01937-13;
RA   Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA   Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA   Amann R.I., Teeling H.;
RT   "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT   KMM 3901T reveals a broad potential for degradation of algal
RT   polysaccharides.";
RL   Appl. Environ. Microbiol. 79:6813-6822(2013).
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; HG315671; CDF78284.1; -; Genomic_DNA.
DR   RefSeq; WP_038527308.1; NZ_HG315671.1.
DR   AlphaFoldDB; T2KJW3; -.
DR   STRING; 1347342.BN863_5720; -.
DR   PATRIC; fig|1347342.6.peg.576; -.
DR   eggNOG; COG0093; Bacteria.
DR   HOGENOM; CLU_095071_2_1_10; -.
DR   OrthoDB; 9806379at2; -.
DR   Proteomes; UP000016160; 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:UP000016160};
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|HAMAP-Rule:MF_01367,
KW   ECO:0000256|RuleBase:RU003950};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01367,
KW   ECO:0000256|RuleBase:RU003950}.
SQ   SEQUENCE   122 AA;  13370 MW;  25BC9B5802CA63F1 CRC64;
     MLQQESRLKV ADNTGAKEVL TIRVLGGTKR RYASVGDKIV VSVKDATPNG NIKKGAVSTA
     VVVRTVKEVR RPDGSYIRFD DNACVLLNPT GEMRGTRVFG PVARELRDKQ FMKIVSLAPE
     VL
//
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