RL23_THETH
ID RL23_THETH Reviewed; 96 AA.
AC Q9RA57;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
DE Short=L*23;
GN Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369};
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;
RA Dontsova M.V., Shcherbakov D.V., Garber M.B.;
RT "Overexpression of the gene of ribosomal protein L23 from Thermus
RT thermophilus and crystallization of the recombinant protein.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=12766408; DOI=10.1023/a:1023502307069;
RA Oehman A., Rak A., Dontsova M., Garber M.B., Haerd T.;
RT "NMR structure of the ribosomal protein L23 from Thermus thermophilus.";
RL J. Biomol. NMR 26:131-137(2003).
CC -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA. One of
CC the proteins that surrounds the polypeptide exit tunnel on the outside
CC of the ribosome. Forms the main docking site for trigger factor binding
CC to the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29, and
CC trigger factor when it is bound to the ribosome. {ECO:0000255|HAMAP-
CC Rule:MF_01369}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000255|HAMAP-Rule:MF_01369}.
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DR EMBL; AF094532; AAD55971.1; -; Genomic_DNA.
DR RefSeq; WP_008633421.1; NZ_LR027517.1.
DR PDB; 1N88; NMR; -; A=1-96.
DR PDB; 4V4X; X-ray; 5.00 A; BW=1-96.
DR PDB; 4V4Y; X-ray; 5.50 A; BW=1-96.
DR PDB; 4V4Z; X-ray; 4.51 A; BW=1-96.
DR PDBsum; 1N88; -.
DR PDBsum; 4V4X; -.
DR PDBsum; 4V4Y; -.
DR PDBsum; 4V4Z; -.
DR AlphaFoldDB; Q9RA57; -.
DR BMRB; Q9RA57; -.
DR SMR; Q9RA57; -.
DR GeneID; 3168722; -.
DR OMA; FEVDHRA; -.
DR EvolutionaryTrace; Q9RA57; -.
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; 3.30.70.330; -; 1.
DR HAMAP; MF_01369_B; Ribosomal_L23_B; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR11620; PTHR11620; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..96
FT /note="50S ribosomal protein L23"
FT /id="PRO_0000129428"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:1N88"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1N88"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:1N88"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:1N88"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:1N88"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:1N88"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:1N88"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1N88"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:1N88"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:1N88"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1N88"
SQ SEQUENCE 96 AA; 10737 MW; 28ABA3C2D83A102A CRC64;
MKTAYDVILA PVLSEKAYAG FAEGKYTFWV HPKATKTEIK NAVETAFKVK VVKVNTLHVR
GKKKRLGRYL GKRPDRKKAI VQVAPGQKIE ALEGLI
