ID   RL14_STAHJ              Reviewed;         122 AA.
AC   Q4L8A4;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367};
GN   Name=rplN {ECO:0000255|HAMAP-Rule:MF_01367}; OrderedLocusNames=SH0812;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit bridges in
CC       the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}.
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:0000255|HAMAP-Rule:MF_01367}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01367}.
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DR   EMBL; AP006716; BAE04121.1; -; Genomic_DNA.
DR   RefSeq; WP_002466492.1; NC_007168.1.
DR   AlphaFoldDB; Q4L8A4; -.
DR   SMR; Q4L8A4; -.
DR   STRING; 279808.SH0812; -.
DR   EnsemblBacteria; BAE04121; BAE04121; SH0812.
DR   GeneID; 58063005; -.
DR   KEGG; sha:SH0812; -.
DR   eggNOG; COG0093; Bacteria.
DR   HOGENOM; CLU_095071_2_1_9; -.
DR   OMA; AKEVLCI; -.
DR   OrthoDB; 1799923at2; -.
DR   Proteomes; UP000000543; 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; -; 1.
DR   HAMAP; MF_01367; Ribosomal_L14; 1.
DR   InterPro; IPR036853; Ribosomal_L14_sf.
DR   InterPro; IPR000218; Ribosomal_L14P.
DR   InterPro; IPR005745; Ribosomal_L14P_bac-type.
DR   InterPro; IPR019972; Ribosomal_L14P_CS.
DR   PANTHER; PTHR11761; PTHR11761; 1.
DR   Pfam; PF00238; Ribosomal_L14; 1.
DR   SMART; SM01374; Ribosomal_L14; 1.
DR   SUPFAM; SSF50193; SSF50193; 1.
DR   TIGRFAMs; TIGR01067; rplN_bact; 1.
DR   PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..122
FT                   /note="50S ribosomal protein L14"
FT                   /id="PRO_0000224020"
SQ   SEQUENCE   122 AA;  13121 MW;  D9190728BC0B7871 CRC64;
     MIQQETRLKV ADNSGAREVL TIKVLGGSGR KTANIGDVIV CTVKNATPGG VVKKGDVVKA
     VVVRTKSGVR RNDGSYIKFD ENACVIIRDD KGPRGTRIFG PVARELREGN FMKIVSLAPE
     VL