ID   RL4_PSEMY               Reviewed;         200 AA.
AC   A4XZ89;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Pmen_3908;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC       initially binds near the 5'-end of the 23S rRNA. It is important during
CC       the early stages of 50S assembly. It makes multiple contacts with
CC       different domains of the 23S rRNA in the assembled 50S subunit and
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}.
CC   -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC       {ECO:0000255|HAMAP-Rule:MF_01328}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01328}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01328}.
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DR   EMBL; CP000680; ABP86655.1; -; Genomic_DNA.
DR   RefSeq; WP_003243889.1; NC_009439.1.
DR   AlphaFoldDB; A4XZ89; -.
DR   SMR; A4XZ89; -.
DR   STRING; 399739.Pmen_3908; -.
DR   EnsemblBacteria; ABP86655; ABP86655; Pmen_3908.
DR   GeneID; 57604894; -.
DR   KEGG; pmy:Pmen_3908; -.
DR   PATRIC; fig|399739.8.peg.3961; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_041575_5_2_6; -.
DR   OMA; PQVHILE; -.
DR   OrthoDB; 1572673at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; 3.40.1370.10; -; 1.
DR   HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR   InterPro; IPR002136; Ribosomal_L4/L1e.
DR   InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR   InterPro; IPR013005; Ribosomal_uL4/L1e.
DR   PANTHER; PTHR10746; PTHR10746; 1.
DR   Pfam; PF00573; Ribosomal_L4; 1.
DR   SUPFAM; SSF52166; SSF52166; 1.
DR   TIGRFAMs; TIGR03953; rplD_bact; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..200
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_1000052472"
FT   REGION          38..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   200 AA;  21557 MW;  683E59FCD439282C CRC64;
     MQLNVNGAQA IEVSDATFGG EFNETLVHQA VVAYMAGGRQ GTKGQKSRSD VSGGGKRPWR
     QKGTGRARAG TTRGPIWRGG GVTFAASTRN HDQKLNKKMY RAALRSILAE LVRTDRLVVV
     EDFAVEAPKT KALLSKLNGL GLNDVLIVSD AVDQNLYLAA RNLPHVDVRD VQGSDPVSLI
     AYEKVLVTVS AVKKFEELLG