ID   RL4_MARMM               Reviewed;         211 AA.
AC   Q0ANQ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Mmar10_1794;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC   Maricaulis.
OX   NCBI_TaxID=394221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA   Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000449; ABI66086.1; -; Genomic_DNA.
DR   RefSeq; WP_011643732.1; NC_008347.1.
DR   AlphaFoldDB; Q0ANQ1; -.
DR   SMR; Q0ANQ1; -.
DR   STRING; 394221.Mmar10_1794; -.
DR   EnsemblBacteria; ABI66086; ABI66086; Mmar10_1794.
DR   KEGG; mmr:Mmar10_1794; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_041575_5_1_5; -.
DR   OMA; PQVHILE; -.
DR   OrthoDB; 1572673at2; -.
DR   Proteomes; UP000001964; 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..211
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_1000052435"
FT   REGION          63..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   211 AA;  22654 MW;  FE7E581FF93D3926 CRC64;
     MKIEVKTLAA KDAGAIDLDD AVFGIEEVRS DLLQRVVKWQ LAARQQGTHK TLGRSEINRT
     KKRFGRQKGG GTARHGARSA PQFVGGGKAH GPRVRSHAHE LPKKVRALGL RHALSAKLGA
     KSLVIIDDAA LDAPQTKALR TSFEGLGISN ALVISGAEVN ENFAKAARNL PCIDVLPAQG
     LNVYDVLRRD TLVLTKAAVE QIHARLSAKE A