RL25_THETH
ID RL25_THETH Reviewed; 206 AA.
AC P56930; Q7M0Q3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 3.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=50S ribosomal protein L25;
DE Short=TL5;
GN Name=rplY; Synonyms=rpl25, rptL5;
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VK1;
RX PubMed=9150868; DOI=10.1016/s0300-9084(97)86713-2;
RA Gryaznova O.I., Davydova N.L., Gongadze G.M., Jonsson B.-H., Garber M.B.,
RA Liljas A.;
RT "A ribosomal protein from Thermus thermophilus is homologous to a general
RT shock protein.";
RL Biochimie 78:915-919(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-53 AND 82-90, AND CHARACTERIZATION OF 5S RRNA
RP BINDING.
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 IDENTIFICATION OF FUNCTIONAL DOMAINS.
RC STRAIN=VK1;
RX PubMed=10356982; DOI=10.1016/s0014-5793(99)00538-4;
RA Gongadze G.M., Meshcheryakov V.A., Serganov A.A., Fomenkova N.P.,
RA Mudrik E.S., Jonsson B.H., Liljas A., Nikonov S.V., Garber M.B.;
RT "N-terminal domain, residues 1-91, of ribosomal protein TL5 from Thermus
RT thermophilus binds specifically and strongly to the region of 5S rRNA
RT containing loop E.";
RL FEBS Lett. 451:51-55(1999).
RN [4]
RP SUBSTITUTES FOR L25 IN E.COLI.
RX PubMed=11109964;
RA Zvereva M.E., Shpanchenko O.V., Nierhaus K., Dontsova O.A.;
RT "Ribosomal protein TL5 of T. thermophilus is incorporated in the E. coli
RT 50S ribosomal subunit.";
RL Dokl. Biochem. 374:199-201(2000).
RN [5]
RP MUTAGENESIS OF 5S RRNA CONTACTING RESIDUES IN A TRUNCATED PROTEIN (RESIDUES
RP 1-91).
RX PubMed=15718233; DOI=10.1074/jbc.m413596200;
RA Gongadze G.M., Korepanov A.P., Stolboushkina E.A., Zelinskaya N.V.,
RA Korobeinikova A.V., Ruzanov M.V., Eliseev B.D., Nikonov O.S., Nikonov S.V.,
RA Garber M.B., Lim V.I.;
RT "The crucial role of conserved intermolecular H-bonds inaccessible to the
RT solvent in formation and stabilization of the TL5.5 SrRNA complex.";
RL J. Biol. Chem. 280:16151-16156(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=11418764; DOI=10.1107/s0907444901006291;
RA Fedorov R., Meshcheryakov V., Gongadze G., Fomenkova N., Nevskaya N.,
RA Selmer M., Laurberg M., Kristensen O., Al-Karadaghi S., Liljas A.,
RA Garber M.B., Nikonov S.;
RT "Structure of ribosomal protein TL5 complexed with RNA provides new
RT insights into the CTC family of stress proteins.";
RL Acta Crystallogr. D 57:968-976(2001).
CC -!- FUNCTION: This is one of 3 proteins that mediate the attachment of the
CC 5S rRNA onto the large ribosomal subunit.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts the 5S rRNA.
CC -!- DOMAIN: The N-terminal 91 amino acids are capable of binding to 5S rRNA
CC and also of displacing full-length protein bound to 5S rRNA. The first
CC 80 amino acids are not sufficient.
CC -!- MISCELLANEOUS: Despite its considerably larger size this protein can
CC substitute for the endogenous E.coli L25 protein in vitro.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family. CTC
CC subfamily. {ECO:0000305}.
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DR EMBL; X94435; CAA64209.1; -; Genomic_DNA.
DR PIR; S68792; S68792.
DR PDB; 1FEU; X-ray; 2.30 A; A/D=1-206.
DR PDBsum; 1FEU; -.
DR AlphaFoldDB; P56930; -.
DR SMR; P56930; -.
DR EvolutionaryTrace; P56930; -.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0008097; F:5S rRNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00495; Ribosomal_L25_TL5_CTC; 1.
DR Gene3D; 2.170.120.20; -; 1.
DR Gene3D; 2.40.240.10; -; 1.
DR HAMAP; MF_01334; Ribosomal_L25_CTC; 1.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR029751; Ribosomal_L25.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR020057; Ribosomal_L25_b-dom.
DR InterPro; IPR037121; Ribosomal_L25_C.
DR InterPro; IPR001021; Ribosomal_L25_long.
DR Pfam; PF01386; Ribosomal_L25p; 1.
DR Pfam; PF14693; Ribosomal_TL5_C; 1.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00731; bL25_bact_ctc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..206
FT /note="50S ribosomal protein L25"
FT /id="PRO_0000181609"
FT REGION 1..91
FT /note="L25 domain"
FT REGION 92..206
FT /note="CTC domain"
FT REGION 184..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 10
FT /note="R->A: Destabilizes formation of the 5S rRNA/N-
FT terminal TL5 complex."
FT /evidence="ECO:0000269|PubMed:15718233"
FT MUTAGEN 14
FT /note="K->A: No effect on 5S rRNA/N-terminal TL5 complex
FT formation."
FT /evidence="ECO:0000269|PubMed:15718233"
FT MUTAGEN 16
FT /note="S->A: No effect on 5S rRNA/N-terminal TL5 complex
FT formation."
FT /evidence="ECO:0000269|PubMed:15718233"
FT MUTAGEN 19
FT /note="R->A: Destabilizes formation of the 5S rRNA/N-
FT terminal TL5 complex."
FT /evidence="ECO:0000269|PubMed:15718233"
FT MUTAGEN 20
FT /note="R->A: No effect on 5S rRNA/N-terminal TL5 complex
FT formation."
FT /evidence="ECO:0000269|PubMed:15718233"
FT MUTAGEN 29
FT /note="Y->F,R,S: No 5S rRNA/N-terminal TL5 complex formed."
FT /evidence="ECO:0000269|PubMed:15718233"
FT MUTAGEN 85
FT /note="H->A,N,T: Destabilizes formation of the 5S rRNA/N-
FT terminal TL5 complex."
FT /evidence="ECO:0000269|PubMed:15718233"
FT MUTAGEN 85
FT /note="H->F: No 5S rRNA/N-terminal TL5 complex formed."
FT /evidence="ECO:0000269|PubMed:15718233"
FT MUTAGEN 87
FT /note="D->E: Strongly destabilizes formation of the 5S
FT rRNA/N-terminal TL5 complex."
FT /evidence="ECO:0000269|PubMed:15718233"
FT MUTAGEN 87
FT /note="D->N,S: No 5S rRNA/N-terminal TL5 complex formed."
FT /evidence="ECO:0000269|PubMed:15718233"
FT CONFLICT 27
FT /note="L -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1FEU"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1FEU"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:1FEU"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 96..106
FT /evidence="ECO:0007829|PDB:1FEU"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:1FEU"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1FEU"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1FEU"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1FEU"
SQ SEQUENCE 206 AA; 23219 MW; E6C214CAF141316C CRC64;
MEYRLKAYYR EGEKPSALRR AGKLPGLMYN RHLNRKVYVD LVEFDKVFRQ ASIHHVIVLE
LPDGQSLPTL VRQVNLDKRR RRPEHVDFFV LSDEPVEMYV PLRFVGTPAG VRAGGVLQEI
HRDILVKVSP RNIPEFIEVD VSGLEIGDSL HASDLKLPPG VELAVSPEET IAAVVPPEDV
EKLAEEAAAE VAEPEVIKKG KEEEEE
