ID   RL14_FINM2              Reviewed;         122 AA.
AC   B0RZR9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367};
GN   Name=rplN {ECO:0000255|HAMAP-Rule:MF_01367}; OrderedLocusNames=FMG_0165;
OS   Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS   (Peptostreptococcus magnus).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=334413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29328 / DSM 20472 / WAL 2508;
RX   PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA   Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA   Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT   "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT   pathogen.";
RL   DNA Res. 15:39-47(2008).
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; AP008971; BAG07583.1; -; Genomic_DNA.
DR   RefSeq; WP_002836120.1; NC_010376.1.
DR   AlphaFoldDB; B0RZR9; -.
DR   SMR; B0RZR9; -.
DR   STRING; 334413.FMG_0165; -.
DR   PRIDE; B0RZR9; -.
DR   EnsemblBacteria; BAG07583; BAG07583; FMG_0165.
DR   GeneID; 60839400; -.
DR   KEGG; fma:FMG_0165; -.
DR   eggNOG; COG0093; Bacteria.
DR   HOGENOM; CLU_095071_2_1_9; -.
DR   OMA; AKEVLCI; -.
DR   OrthoDB; 1799923at2; -.
DR   Proteomes; UP000001319; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..122
FT                   /note="50S ribosomal protein L14"
FT                   /id="PRO_1000144274"
SQ   SEQUENCE   122 AA;  13196 MW;  6A2DA1D36A105923 CRC64;
     MIQQESRLRV ADNSGAKELL VIRVLGGTKR KYAAIGDIVV CSVKSAQPGG MVKKGDVVKA
     VIVRTTKPLG RADGSYIRFD DNAAVIIKDD KNPVGTRIFG SVTRELRANN FMKIISLAPE
     VL