ID   RL4_TREPS               Reviewed;         216 AA.
AC   B2S2D7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=TPASS_0190;
OS   Treponema pallidum subsp. pallidum (strain SS14).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=455434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS14;
RX   PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA   Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA   Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA   Molla M.N., Albert T.J., Weinstock G.M.;
RT   "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT   determined with oligonucleotide arrays.";
RL   BMC Microbiol. 8:76-76(2008).
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; CP000805; ACD70616.1; -; Genomic_DNA.
DR   RefSeq; WP_010881637.1; NC_021508.1.
DR   AlphaFoldDB; B2S2D7; -.
DR   SMR; B2S2D7; -.
DR   EnsemblBacteria; ACD70616; ACD70616; TPASS_0190.
DR   KEGG; tpp:TPASS_0190; -.
DR   PATRIC; fig|455434.6.peg.193; -.
DR   OMA; PQVHILE; -.
DR   Proteomes; UP000001202; 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..216
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_1000142202"
FT   REGION          51..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   216 AA;  24179 MW;  288BE5E35151CB0A CRC64;
     MEKTVYSVEG VALRSVELDE SVFGLSVNRG VIYYAINSEL SNKRLGTACT KGRSEVHGSN
     TKPYKQKGTG RARRGDKKSP LLVGGGTIFG PKPRDFHYAL PKKVKRLAMK SLLSLKAQGD
     ALTVIEDFTV ESGKTRDLIQ VLRHFAQRER TVFILQNDDA LLKRAGRNIP TLSFLSYNRL
     RAHDLFYGRK VLVLETAVHK IADFYRSKDA AQDGTY