RL5_THETH
ID RL5_THETH Reviewed; 182 AA.
AC P41201;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=50S ribosomal protein L5;
DE AltName: Full=TL4;
DE AltName: Full=TthL5;
GN Name=rplE; Synonyms=rpl5;
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33923 / DSM 674 / AT-62;
RX PubMed=1764514; DOI=10.1016/0300-9084(91)90046-4;
RA Jahn O., Hartmann R.K., Boeckh T., Erdmann V.A.;
RT "Comparative analysis of ribosomal protein L5 sequences from bacteria of
RT the genus Thermus.";
RL Biochimie 73:669-678(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-40.
RC STRAIN=VK1;
RX PubMed=8647295; DOI=10.1016/0014-5793(96)00457-7;
RA Gongadze G.M., Kashparov I., Lorenz S., Schroeder W., Erdmann V.A.,
RA Liljas A., Garber M.B.;
RT "5S rRNA binding ribosomal proteins from Thermus thermophilus:
RT identification and some structural properties.";
RL FEBS Lett. 386:260-262(1996).
RN [3]
RP BINDING TO 5S RRNA.
RC STRAIN=VK1;
RX PubMed=11524947; DOI=10.1023/A:1010562707875;
RA Gongadze G.M., Perederina A.A., Meshcheriakov V.A., Fedorov R.V.,
RA Moskalenko S.E., Rak A.V., Serganov A.A., Shcherbakov D.V., Nikonov S.V.,
RA Garber M.B.;
RT "The Thermus thermophilus 5S rRNA-protein complex: identification of
RT specific binding sites for proteins L5 and L18 in 5S rRNA.";
RL Mol. Biol. (Mosk.) 35:610-616(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF THE PROTEIN IN COMPLEX WITH A 5S
RP RRNA FRAGMENT.
RC STRAIN=VK1;
RX PubMed=12515387;
RA Perederina A., Nevskaya N., Nikonov O., Nikulin A., Dumas P., Yao M.,
RA Tanaka I., Garber M.B., Gongadze G., Nikonov S.;
RT "Detailed analysis of RNA-protein interactions within the bacterial
RT ribosomal protein L5/5S rRNA complex.";
RL RNA 8:1548-1557(2002).
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 (forming bridge B1b) connecting the head
CC of the 30S subunit to the top of the 50S subunit. The bridge itself
CC contacts the P site tRNA and is implicated in movement during ribosome
CC translocation. Also contacts the P site tRNA independently of the
CC intersubunit bridge; the 5S rRNA and some of its associated proteins
CC might help stabilize positioning of ribosome-bound tRNAs (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a bridge to the 30S subunit in the 70S ribosome,
CC contacting protein S13; this bridge is straddled by the 5S rRNA.
CC Contacts the P site tRNA (By similarity). Part of the 50S ribosomal
CC subunit; part of the 5S rRNA/L5/L18/L25 (TL5) subcomplex. {ECO:0000250,
CC ECO:0000269|PubMed:12515387}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S77826; AAB21093.1; -; Genomic_DNA.
DR RefSeq; WP_011228843.1; NZ_AP019801.1.
DR PDB; 1MJI; X-ray; 2.50 A; A/B=1-182.
DR PDB; 4V4X; X-ray; 5.00 A; BG=1-182.
DR PDB; 4V4Y; X-ray; 5.50 A; BG=1-182.
DR PDB; 4V4Z; X-ray; 4.51 A; BG=1-182.
DR PDB; 5NS3; X-ray; 2.40 A; A/B=5-181.
DR PDB; 5NS4; X-ray; 2.40 A; A/B=4-181.
DR PDBsum; 1MJI; -.
DR PDBsum; 4V4X; -.
DR PDBsum; 4V4Y; -.
DR PDBsum; 4V4Z; -.
DR PDBsum; 5NS3; -.
DR PDBsum; 5NS4; -.
DR AlphaFoldDB; P41201; -.
DR SMR; P41201; -.
DR GeneID; 3169803; -.
DR EvolutionaryTrace; P41201; -.
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; Direct protein sequencing; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8647295"
FT CHAIN 2..182
FT /note="50S ribosomal protein L5"
FT /id="PRO_0000125015"
FT CONFLICT 5
FT /note="V -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="R -> RE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:5NS3"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:5NS3"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5NS3"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:5NS3"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1MJI"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:5NS3"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5NS3"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1MJI"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:5NS3"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:5NS3"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:5NS3"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5NS3"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:5NS3"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1MJI"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:5NS3"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:5NS3"
SQ SEQUENCE 182 AA; 21030 MW; 69A3361F6825929B CRC64;
MPLDVALKRK YYEEVRPELI RRFGYQNVWE VPRLEKVVIN QGLGEAKEDA RILEKAAQEL
ALITGQKPAV TRAKKSISNF KLRKGMPIGL RVTLRRDRMW IFLEKLLNVA LPRIRDFRGL
NPNSFDGRGN YNLGLREQLI FPEITYDMVD ALRGMDIAVV TTAETDEEAR ALLELLGFPF
RK
