ID D2TMJ3_CITRI Unreviewed; 123 AA.
AC D2TMJ3;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Large ribosomal subunit protein uL14 {ECO:0000256|HAMAP-Rule:MF_01367};
GN Name=rplN {ECO:0000256|HAMAP-Rule:MF_01367};
GN OrderedLocusNames=ROD_45112 {ECO:0000313|EMBL:CBG91207.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG91207.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG91207.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG91207.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN543502; CBG91207.1; -; Genomic_DNA.
DR RefSeq; WP_002919748.1; NC_013716.1.
DR AlphaFoldDB; D2TMJ3; -.
DR SMR; D2TMJ3; -.
DR STRING; 637910.ROD_45112; -.
DR GeneID; 84234847; -.
DR KEGG; cro:ROD_45112; -.
DR eggNOG; COG0093; Bacteria.
DR HOGENOM; CLU_095071_2_1_6; -.
DR OrthoDB; 9806379at2; -.
DR Proteomes; UP000001889; 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 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 123 AA; 13555 MW; 582ACB16239094BB CRC64;
MIQEQTMLNV ADNSGARRVM CIKVLGGSHR RYAGVGDIIK ITIKEAIPRG KVKKGDVLKA
VVVRTKKGVR RPDGSVIRFD GNACVILNNN SEQPIGTRIF GPVTRELRTE KFMKIISLAP
EVL
//
