RL5_THET2
ID RL5_THET2 Reviewed; 182 AA.
AC Q72I16;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=TT_C1316;
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: This is 1 of the proteins that binds and probably mediates
CC the attachment of the 5S RNA into the large ribosomal subunit, where it
CC forms part of the central protuberance. In the 70S ribosome it contacts
CC protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits;
CC this bridge is implicated in subunit movement. Contacts the P site
CC tRNA; the 5S rRNA and some of its associated proteins might help
CC stabilize positioning of ribosome-bound tRNAs. {ECO:0000255|HAMAP-
CC Rule:MF_01333}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA.
CC Forms a bridge to the 30S subunit in the 70S ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_01333}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000255|HAMAP-Rule:MF_01333}.
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DR EMBL; AE017221; AAS81658.1; -; Genomic_DNA.
DR RefSeq; WP_011173706.1; NC_005835.1.
DR PDB; 4V4I; X-ray; 3.71 A; E=1-182.
DR PDB; 4V4J; X-ray; 3.83 A; E=1-182.
DR PDB; 4V63; X-ray; 3.21 A; BG/DG=1-182.
DR PDB; 4V67; X-ray; 3.00 A; BG/DG=1-182.
DR PDB; 4V7P; X-ray; 3.62 A; BF/CF=2-182.
DR PDB; 4V83; X-ray; 3.50 A; BF/DF=2-182.
DR PDB; 4V84; X-ray; 3.40 A; BF/DF=2-182.
DR PDB; 4V9J; X-ray; 3.86 A; BG/DG=2-182.
DR PDB; 4V9K; X-ray; 3.50 A; BG/DG=2-182.
DR PDB; 4V9L; X-ray; 3.50 A; BG/DG=2-182.
DR PDB; 4V9M; X-ray; 4.00 A; BG/DG=2-182.
DR PDB; 4V9N; X-ray; 3.40 A; BG/DG=2-182.
DR PDB; 4V9Q; X-ray; 3.40 A; AG/CG=2-182.
DR PDB; 4W29; X-ray; 3.80 A; BG/DG=2-182.
DR PDB; 4XEJ; X-ray; 3.80 A; AL05/BL05=2-182.
DR PDB; 5J4D; X-ray; 3.10 A; H/MB=1-182.
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; Q72I16; -.
DR SMR; Q72I16; -.
DR IntAct; Q72I16; 4.
DR STRING; 262724.TT_C1316; -.
DR EnsemblBacteria; AAS81658; AAS81658; TT_C1316.
DR KEGG; tth:TT_C1316; -.
DR eggNOG; COG0094; Bacteria.
DR HOGENOM; CLU_061015_2_1_0; -.
DR OMA; ERMYAFL; -.
DR OrthoDB; 1456375at2; -.
DR EvolutionaryTrace; Q72I16; -.
DR Proteomes; UP000000592; Chromosome.
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:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1440.10; -; 1.
DR HAMAP; MF_01333_B; Ribosomal_L5_B; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR020930; Ribosomal_L5_bac-type.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR020929; Ribosomal_L5_CS.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
DR PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..182
FT /note="50S ribosomal protein L5"
FT /id="PRO_0000125013"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4V84"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4V63"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:4V67"
SQ SEQUENCE 182 AA; 21044 MW; C3A8E0CFD884EEEA CRC64;
MPLDLALKRK YYEEVRPELI RRFGYQNVWE VPRLEKVVIN QGLGEAKEDA RILEKAAQEL
ALITGQKPAV TRAKKSISNF KLRKGMPIGL RVTLRRDRMW IFLEKLLNVA LPRIRDFRGL
NPNSFDGRGN YNLGLREQLI FPEITYDMVD ALRGMDIAVV TTAETDEEAR ALLELLGFPF
RK
