RL4_GEOSE
ID RL4_GEOSE Reviewed; 207 AA.
AC P28601;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=50S ribosomal protein L4;
DE Short=BL4;
GN Name=rplD;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=799;
RX PubMed=1499563; DOI=10.1111/j.1432-1033.1992.tb17119.x;
RA Herwig S., Kruft V., Wittmann-Liebold B.;
RT "Primary structures of ribosomal proteins L3 and L4 from Bacillus
RT stearothermophilus.";
RL Eur. J. Biochem. 207:877-885(1992).
RN [2]
RP PROTEIN SEQUENCE OF 53-64 AND 66-75, AND CROSS-LINKING TO RRNA.
RC STRAIN=799;
RX PubMed=7556101; DOI=10.1002/j.1460-2075.1995.tb00137.x;
RA Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
RT "Protein-rRNA binding features and their structural and functional
RT implications in ribosomes as determined by cross-linking studies.";
RL EMBO J. 14:4578-4588(1995).
RN [3]
RP ISOLATION OF ANTIBIOTIC RESISTANT STRAINS.
RC STRAIN=799;
RX PubMed=2254291; DOI=10.1128/jb.172.12.7306-7309.1990;
RA Schnier J., Gewitz H.S., Behrens S.E., Lee A., Ginther C., Leighton T.;
RT "Isolation and characterization of Bacillus stearothermophilus 30S and 50S
RT ribosomal protein mutations.";
RL J. Bacteriol. 172:7306-7309(1990).
RN [4]
RP ABILITY TO REPRESS THE E.COLI S10 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).
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: This protein when expressed in E.coli represses the
CC endogenous S10 operon; this may not occur in B.stearothermophilus
CC however.
CC -!- FUNCTION: Forms part of the polypeptide exit tunnel. {ECO:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- MISCELLANEOUS: Erythromycin, niddamycin, oleandomycin and spiramycin-
CC resistant strains have changes in this protein as seen by gel
CC electrophoresis; the nature of these changes has not been determined.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000305}.
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DR EMBL; X67014; CAA47403.1; -; Genomic_DNA.
DR PIR; S24364; S24364.
DR RefSeq; WP_033008661.1; NZ_RCTK01000011.1.
DR AlphaFoldDB; P28601; -.
DR SMR; P28601; -.
DR GeneID; 58573163; -.
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:0046677; P:response to antibiotic; 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 1: Evidence at protein level;
KW Antibiotic resistance; Direct protein sequencing; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..207
FT /note="50S ribosomal protein L4"
FT /id="PRO_0000129182"
FT REGION 44..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 207 AA; 22810 MW; 4ED00DDFC493A376 CRC64;
MPKVALYNQN GQTVGEIELN DAVFGIEPNK HVLFEAVIMQ RASMRQGTHK TKNRAEVSGG
GRKPWRQKGT GRARQGSIRA PQWRGGGTVF GPVPRSYSYK LPKKVRRLAI KSALSSKVLE
NDIVVLDQLS LEAPKTKEMV KILNNLSVDR KALIVTDELN ENVYLSARNI PGVKVVPANG
INVLDVLNHD KLVITKAAVE KVEEVLA