ID A0A3P1S6D4_9FIRM Unreviewed; 122 AA.
AC A0A3P1S6D4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=EII25_03735 {ECO:0000313|EMBL:RRC92798.1};
OS Erysipelotrichaceae bacterium OH741_COT-311.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=2491058 {ECO:0000313|EMBL:RRC92798.1, ECO:0000313|Proteomes:UP000270315};
RN [1] {ECO:0000313|EMBL:RRC92798.1, ECO:0000313|Proteomes:UP000270315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH741_COT-311 {ECO:0000313|EMBL:RRC92798.1,
RC ECO:0000313|Proteomes:UP000270315};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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}.
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:RRC92798.1}.
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DR EMBL; RQZE01000005; RRC92798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1S6D4; -.
DR OrthoDB; 9806379at2; -.
DR Proteomes; UP000270315; Unassembled WGS sequence.
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:UP000270315};
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; 13242 MW; F590DAF6D9E32554 CRC64;
MIQNETRLKV ADNTGAKELL VIRCLGGSKR RNANIGDIIV CSVKQASPGG SVKKGDVVKA
VVVRTKYGIA RENGSYIKFD DNAAVIIKDD NSPKGTRIFG PVARELREKD FMKIVSLAPE
VL
//
