ID   RL4_MORMO               Reviewed;         200 AA.
AC   P49226;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=50S ribosomal protein L4;
GN   Name=rplD;
OS   Morganella morganii (Proteus morganii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Morganella.
OX   NCBI_TaxID=582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ABILITY TO REPRESS THE E.COLI S10
RP   OPERON.
RX   PubMed=8722027; DOI=10.1139/o95-119;
RA   Zengel J.M., Vorozheikina D., Li X., Lindahl L.;
RT   "Regulation of the Escherichia coli S10 ribosomal protein operon by
RT   heterologous L4 ribosomal proteins.";
RL   Biochem. Cell Biol. 73:1105-1112(1995).
RN   [2]
RP   EVIDENCE FOR REGULATION OF THE S10 OPERON.
RX   PubMed=10498727; DOI=10.1128/jb.181.19.6124-6132.1999;
RA   Allen T., Shen P., Samsel L., Liu R., Lindahl L., Zengel J.M.;
RT   "Phylogenetic analysis of L4-mediated autogenous control of the S10
RT   ribosomal protein operon.";
RL   J. Bacteriol. 181:6124-6132(1999).
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: Protein L4 is a both a transcriptional repressor and a
CC       translational repressor protein. It regulates transcription of the S10
CC       operon (to which L4 belongs) by causing premature termination of
CC       transcription within the S10 leader. L4 controls the translation of the
CC       S10 operon by binding to its mRNA (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: This protein when expressed in E.coli represses both
CC       transcription and translation of the endogenous S10 operon. As the
CC       M.morganii S10 leader can be regulated in vitro by the E.coli L4
CC       protein this strongly suggests the endogenous protein controls its own
CC       S10 operon in a similar fashion.
CC   -!- FUNCTION: Forms part of the polypeptide exit tunnel. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000305}.
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DR   EMBL; U37798; AAB41513.1; -; Genomic_DNA.
DR   AlphaFoldDB; P49226; -.
DR   SMR; P49226; -.
DR   STRING; 582.AL531_14830; -.
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:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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   Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   Transcription; Transcription regulation; Transcription termination;
KW   Translation regulation.
FT   CHAIN           1..200
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_0000129235"
FT   REGION          44..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   200 AA;  22140 MW;  0710870E2BFC42F9 CRC64;
     MELVMKDAQS LTVSETTFGR DFNEALVHQV VVAYAAGARQ GTRAQKTRAE VTGSGKKPWR
     QKGTGRARSG SIKSPIWRSG GITFAAKPQD HSQKVNKKMY RGALKSILSE LVRQDRLIIV
     EKFAVEAPKT KLLVQKLKDM ALEDVMIVTH EVDENLFLAA RNLYKVDVRD VTAIDPVSLI
     AFGKVVMTAE AVKQVEEMLA