ID   RL4_CUTAK               Reviewed;         301 AA.
AC   Q6A6M7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=50S ribosomal protein L4;
GN   Name=rplD; OrderedLocusNames=PPA1862;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Forms part of the polypeptide exit tunnel. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000305}.
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DR   EMBL; AE017283; AAT83586.1; -; Genomic_DNA.
DR   RefSeq; WP_002531292.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6A6M7; -.
DR   SMR; Q6A6M7; -.
DR   STRING; 267747.PPA1862; -.
DR   EnsemblBacteria; AAT83586; AAT83586; PPA1862.
DR   KEGG; pac:PPA1862; -.
DR   PATRIC; fig|267747.3.peg.1918; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_041575_5_0_11; -.
DR   OMA; PQVHILE; -.
DR   Proteomes; UP000000603; 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..301
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_0000242414"
FT   REGION          1..223
FT                   /note="50S ribosomal protein L4"
FT   REGION          49..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..301
FT                   /note="Unknown"
SQ   SEQUENCE   301 AA;  32297 MW;  B14A6E8711B13D48 CRC64;
     MNETKTIDVL DVKGKKAGSA ELPGDLFDVN TNIPLIHQVV VAQLAAARQG THATKTRGQV
     SGGGKKPWRQ KGTGRARQGS TRAPQWVGGG TVHGPQPRSY AQRTPKKMVG AALRGALSDM
     ARDNRIFVVT SLVDGDKPST KQAKAVLSGL AELRKVLVVL DRSDEIDWLS VRNLSEVHVL
     AADQLNTYDV VNARTIVFSQ AGLDAFVGAR SANTQALSAQ PEVPETNVAD QHPYGEDSFR
     GDNPPAGFDI KGNEDSMKFH EPSSPWYGRT IAEVWFRSAA AAEAAGFVNA VKSDSEKEDA
     K