RL4_THET2
ID RL4_THET2 Reviewed; 205 AA.
AC Q72I05;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=TT_C1327;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(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. {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.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000255|HAMAP-Rule:MF_01328}.
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DR EMBL; AE017221; AAS81669.1; -; Genomic_DNA.
DR RefSeq; WP_011173713.1; NC_005835.1.
DR PDB; 4V4I; X-ray; 3.71 A; D=1-205.
DR PDB; 4V4J; X-ray; 3.83 A; D=1-205.
DR PDB; 4V63; X-ray; 3.21 A; BF/DF=1-205.
DR PDB; 4V67; X-ray; 3.00 A; BF/DF=1-205.
DR PDB; 4V7P; X-ray; 3.62 A; BE/CE=1-205.
DR PDB; 4V83; X-ray; 3.50 A; BE/DE=1-202.
DR PDB; 4V84; X-ray; 3.40 A; BE/DE=1-202.
DR PDB; 4V9J; X-ray; 3.86 A; BF/DF=1-203.
DR PDB; 4V9K; X-ray; 3.50 A; BF/DF=1-203.
DR PDB; 4V9L; X-ray; 3.50 A; BF/DF=1-203.
DR PDB; 4V9M; X-ray; 4.00 A; BF/DF=1-203.
DR PDB; 4V9N; X-ray; 3.40 A; BF/DF=1-202.
DR PDB; 4V9Q; X-ray; 3.40 A; AF/CF=1-202.
DR PDB; 4W29; X-ray; 3.80 A; BF/DF=1-203.
DR PDB; 4XEJ; X-ray; 3.80 A; AL04/BL04=1-202.
DR PDB; 5J4D; X-ray; 3.10 A; G/LB=1-205.
DR PDBsum; 4V4I; -.
DR PDBsum; 4V4J; -.
DR PDBsum; 4V63; -.
DR PDBsum; 4V67; -.
DR PDBsum; 4V7P; -.
DR PDBsum; 4V83; -.
DR PDBsum; 4V84; -.
DR PDBsum; 4V9J; -.
DR PDBsum; 4V9K; -.
DR PDBsum; 4V9L; -.
DR PDBsum; 4V9M; -.
DR PDBsum; 4V9N; -.
DR PDBsum; 4V9Q; -.
DR PDBsum; 4W29; -.
DR PDBsum; 4XEJ; -.
DR PDBsum; 5J4D; -.
DR AlphaFoldDB; Q72I05; -.
DR SMR; Q72I05; -.
DR IntAct; Q72I05; 4.
DR STRING; 262724.TT_C1327; -.
DR EnsemblBacteria; AAS81669; AAS81669; TT_C1327.
DR GeneID; 3167923; -.
DR KEGG; tth:TT_C1327; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_1_0; -.
DR OMA; PQVHILE; -.
DR EvolutionaryTrace; Q72I05; -.
DR Proteomes; UP000000592; 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 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..205
FT /note="50S ribosomal protein L4"
FT /id="PRO_0000242455"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4V9N"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4V84"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:4V63"
FT TURN 125..129
FT /evidence="ECO:0007829|PDB:4V9L"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:4V63"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4V84"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:4V63"
SQ SEQUENCE 205 AA; 22708 MW; FC50A700F8CBC324 CRC64;
MYQIPVLSPS GRRELAADLP AEINPHLLWE VVRWQLAKRR RGTASTKTRG EVAYSGRKIW
PQKHTGRARH GDIGAPIFVG GGVVFGPKPR DYSYTLPKKV RKKGLAMAVA DRAREGKLLL
VEAFAGVNGK TKEFLAWAKE AGLDGSESVL LVTGNELVRR AARNLPWVVT LAPEGLNVYD
IVRTERLVMD LDAWEVFQNR IGGEA
