ID   RL4_PSEU2               Reviewed;         200 AA.
AC   Q4ZMP5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Psyr_4547;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY39577.1; -; Genomic_DNA.
DR   RefSeq; WP_002555489.1; NC_007005.1.
DR   RefSeq; YP_237615.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZMP5; -.
DR   SMR; Q4ZMP5; -.
DR   STRING; 205918.Psyr_4547; -.
DR   EnsemblBacteria; AAY39577; AAY39577; Psyr_4547.
DR   GeneID; 61872120; -.
DR   GeneID; 64463637; -.
DR   GeneID; 65076911; -.
DR   KEGG; psb:Psyr_4547; -.
DR   PATRIC; fig|205918.7.peg.4686; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_041575_5_2_6; -.
DR   OMA; PQVHILE; -.
DR   Proteomes; UP000000426; 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..200
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_0000242419"
FT   REGION          38..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   200 AA;  21941 MW;  99B6F023A126AF0F CRC64;
     MQLNVNDAQA IEVSELTFGG EFNETLVHQA VVAYMAGGRQ GSKQQKTRSD VRGGGKRPWR
     QKGTGRARAG TIRSPIWRGG GTTFAARPQD HTQKLNKKMY RAALRSILAE LVRTDRLVVV
     QDFAVEAPKT KDLLNKLTGM GLTDVLIVSD AVDQNLYLAA RNLPHVDVRD VQGSDPVSLI
     AYDKVLITVS AVKKFEELLG