ID   RL4_VARPS               Reviewed;         206 AA.
AC   C5CP52;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Vapar_4912;
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S110;
RX   PubMed=21183664; DOI=10.1128/jb.00925-10;
RA   Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA   O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA   Ovchinnikova G., Goodwin L., Han C.;
RT   "Complete genome sequence of the metabolically versatile plant growth-
RT   promoting endophyte, Variovorax paradoxus S110.";
RL   J. Bacteriol. 193:1183-1190(2011).
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; CP001635; ACS21516.1; -; Genomic_DNA.
DR   RefSeq; WP_013543942.1; NC_012791.1.
DR   AlphaFoldDB; C5CP52; -.
DR   SMR; C5CP52; -.
DR   STRING; 543728.Vapar_4912; -.
DR   EnsemblBacteria; ACS21516; ACS21516; Vapar_4912.
DR   GeneID; 45059146; -.
DR   KEGG; vap:Vapar_4912; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_041575_5_2_4; -.
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..206
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_1000214594"
FT   REGION          44..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   206 AA;  23053 MW;  C62D434CEA049EC9 CRC64;
     MQLELLNEQG QAASKYDAPE TVFGRDYNED LVHQIVVAFQ ANARQGTRAQ KDREQVKHST
     KKPFKQKGTG RARAGMTSSP LWRGGGRIFP NMPDENFSQK INKKMYRAGM AAIFSQLARE
     GRLAVVDSLT VDSPKTKPLA ARFKAMNLES VLVIAEEVDE NLYLASRNLV NILVVEPRYA
     DPVSLVHYKK VLVTKGAVDK LKEMFA