ID   RL4_PHYMT               Reviewed;         207 AA.
AC   B3QZZ2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=ATP_00342;
OS   Phytoplasma mali (strain AT).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; 16SrX (Apple proliferation group).
OX   NCBI_TaxID=482235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT;
RX   PubMed=18582369; DOI=10.1186/1471-2164-9-306;
RA   Kube M., Schneider B., Kuhl H., Dandekar T., Heitmann K., Migdoll A.M.,
RA   Reinhardt R., Seemueller E.;
RT   "The linear chromosome of the plant-pathogenic mycoplasma 'Candidatus
RT   Phytoplasma mali'.";
RL   BMC Genomics 9:306-306(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; CU469464; CAP18529.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3QZZ2; -.
DR   SMR; B3QZZ2; -.
DR   STRING; 37692.ATP_00342; -.
DR   EnsemblBacteria; CAP18529; CAP18529; ATP_00342.
DR   KEGG; pml:ATP_00342; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_041575_5_2_14; -.
DR   OMA; HVRINKK; -.
DR   Proteomes; UP000002020; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..207
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_1000166019"
FT   REGION          55..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   207 AA;  23526 MW;  2C5722DC81DA2DF5 CRC64;
     MPKYNLINQK GDFLSQIDLD DEIFGISINK QVLYDVVNAQ RASMRQGTHA TKNRALVSGG
     GKKPWRQKGT GRARHGTIRS PLWRGGGVAF GPSPRDYSVK VNQKVRRLAL KMALSWKINN
     KNLILIDNIN LETHKTKEFQ NILDQLNIQQ KTLILTKDLN HNLCLSIRNL SKVLLETVSH
     VSVYQLLSYS TIILTKEAAN YFEENLK