ID   RL4_XYLF2               Reviewed;         202 AA.
AC   B2I8H0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328};
GN   OrderedLocusNames=XfasM23_0434;
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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; CP001011; ACB91881.1; -; Genomic_DNA.
DR   RefSeq; WP_004090094.1; NC_010577.1.
DR   AlphaFoldDB; B2I8H0; -.
DR   SMR; B2I8H0; -.
DR   EnsemblBacteria; ACB91881; ACB91881; XfasM23_0434.
DR   GeneID; 58015988; -.
DR   KEGG; xfn:XfasM23_0434; -.
DR   HOGENOM; CLU_041575_5_2_6; -.
DR   OMA; PQVHILE; -.
DR   Proteomes; UP000001698; Chromosome.
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..202
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_1000142209"
FT   REGION          42..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   202 AA;  21694 MW;  1B60534BBDBA9035 CRC64;
     MDLTIVGSDN TLPVSDVVFG REFSEALVHQ VVVAYRNTAR SGTKAQKSRS QVSGTTKKSK
     KQKGGGARHG ALTAPIFVGG GVAFAAKPRS FSQKVNRKQY RSAICSIFSE LNRQGRLKVV
     DAFDVEVSKT RVFAEKIKSL EVVGSSLLIV SDEISECLSL SSRNLPCVDV RSVQALDPVA
     LVGSDVVVLT VGAVKKIEEW LV