RL5_GEOSE
ID RL5_GEOSE Reviewed; 179 AA.
AC P08895;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=50S ribosomal protein L5;
DE Short=BL5;
DE Short=BstL5;
GN Name=rplE;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=3542562; DOI=10.1016/0014-5793(87)81303-0;
RA Kimura J., Kimura M.;
RT "The complete amino acid sequences of the 5 S rRNA binding proteins L5 and
RT L18 from the moderate thermophile Bacillus stearothermophilus ribosome.";
RL FEBS Lett. 210:85-90(1987).
RN [2]
RP ISOLATION OF 5S RNA-PROTEIN COMPLEXES.
RX PubMed=4567807; DOI=10.1007/bf00272091;
RA Horne J.R., Erdmann V.A.;
RT "Isolation and characterization of 5S RNA-protein complexes from Bacillus
RT stearothermophilus and Escherichia coli ribosomes.";
RL Mol. Gen. Genet. 119:337-344(1972).
RN [3]
RP MUTAGENESIS OF CONSERVED RESIDUES, AND MASS SPECTROMETRY.
RX PubMed=11866091; DOI=10.1271/bbb.66.103;
RA Iwasaki K., Kikukawa S., Kawamura S., Kouzuma Y., Tanaka I., Kimura M.;
RT "On the interaction of ribosomal protein L5 with 5S rRNA.";
RL Biosci. Biotechnol. Biochem. 66:103-109(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND MUTAGENESIS.
RX PubMed=11350033; DOI=10.1017/s1355838201002345;
RA Nakashima T., Yao M., Kawamura S., Iwasaki K., Kimura M., Tanaka I.;
RT "Ribosomal protein L5 has a highly twisted concave surface and flexible
RT arms responsible for rRNA binding.";
RL RNA 7:692-701(2001).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Contacts the P site tRNA. Forms a bridge to the 30S subunit in
CC the 70S ribosome (By similarity). Part of the 50S ribosomal subunit.
CC Part of the 5S rRNA/L5/L18 subcomplex; in this organism only 2
CC proteins, L5 and L18 have been shown to be part of the 5S rRNA
CC subcomplex, unlike E.coli and T.thermophilus where L25 (TL5) is also
CC found. Has been shown to bind 5S rRNA. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=20090; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11866091};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
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DR PIR; A29102; R5BS5F.
DR RefSeq; WP_033008675.1; NZ_RCTK01000011.1.
DR PDB; 1IQ4; X-ray; 1.80 A; A/B=1-179.
DR PDBsum; 1IQ4; -.
DR AlphaFoldDB; P08895; -.
DR SMR; P08895; -.
DR GeneID; 58573174; -.
DR EvolutionaryTrace; P08895; -.
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 CHAIN 1..179
FT /note="50S ribosomal protein L5"
FT /id="PRO_0000124891"
FT MUTAGEN 33
FT /note="K->A: A 3-fold decrease in binding of the 5S rRNA."
FT MUTAGEN 37
FT /note="N->A: A 25-fold decrease in binding of the 5S rRNA."
FT MUTAGEN 63
FT /note="Q->A: A 12.5-fold decrease in binding of the 5S
FT rRNA."
FT MUTAGEN 77
FT /note="F->A: An 8-fold decrease in binding of the 5S rRNA."
FT MUTAGEN 90
FT /note="T->A: A 4-fold decrease in binding of the 5S rRNA."
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:1IQ4"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:1IQ4"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1IQ4"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:1IQ4"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1IQ4"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:1IQ4"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1IQ4"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1IQ4"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1IQ4"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:1IQ4"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1IQ4"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:1IQ4"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1IQ4"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1IQ4"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:1IQ4"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:1IQ4"
SQ SEQUENCE 179 AA; 20159 MW; 84E1D7BA91C84E8A CRC64;
MNRLKEKYVK EVVPALMSKF NYKSIMQVPK IEKIVINMGV GDAVQNPKAL DSAVEELTLI
AGQRPVVTRA KKSIAGFRLR QGMPIGAKVT LRGERMYEFL DKLISVSLPR VRDFRGVSKK
AFDGRGNYTL GIKEQLIFPE IDYDKVNKVR GMDIVIVTTA NTDEEARELL ALLGMPFQK
