ID   RL20_AQUAE              Reviewed;         118 AA.
AC   O67086;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=50S ribosomal protein L20;
GN   Name=rplT; OrderedLocusNames=aq_952;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the
CC       in vitro assembly process of the 50S ribosomal subunit. It is not
CC       involved in the protein synthesizing functions of that subunit (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family.
CC       {ECO:0000305}.
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DR   EMBL; AE000657; AAC07052.1; -; Genomic_DNA.
DR   PIR; C70382; C70382.
DR   RefSeq; NP_213649.1; NC_000918.1.
DR   RefSeq; WP_010880587.1; NC_000918.1.
DR   PDB; 1GYZ; NMR; -; A=59-118.
DR   PDB; 2GHJ; X-ray; 2.90 A; A/B/D/E=1-118.
DR   PDBsum; 1GYZ; -.
DR   PDBsum; 2GHJ; -.
DR   AlphaFoldDB; O67086; -.
DR   SMR; O67086; -.
DR   STRING; 224324.aq_952; -.
DR   EnsemblBacteria; AAC07052; AAC07052; aq_952.
DR   KEGG; aae:aq_952; -.
DR   PATRIC; fig|224324.8.peg.747; -.
DR   eggNOG; COG0292; Bacteria.
DR   HOGENOM; CLU_123265_0_1_0; -.
DR   InParanoid; O67086; -.
DR   OMA; GRRKNVW; -.
DR   OrthoDB; 1932144at2; -.
DR   EvolutionaryTrace; O67086; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd07026; Ribosomal_L20; 1.
DR   DisProt; DP02143; -.
DR   Gene3D; 1.10.1900.20; -; 1.
DR   HAMAP; MF_00382; Ribosomal_L20; 1.
DR   InterPro; IPR005813; Ribosomal_L20.
DR   InterPro; IPR035566; Ribosomal_protein_L20_C.
DR   PANTHER; PTHR10986; PTHR10986; 1.
DR   Pfam; PF00453; Ribosomal_L20; 1.
DR   PRINTS; PR00062; RIBOSOMALL20.
DR   SUPFAM; SSF74731; SSF74731; 1.
DR   TIGRFAMs; TIGR01032; rplT_bact; 1.
DR   PROSITE; PS00937; RIBOSOMAL_L20; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..118
FT                   /note="50S ribosomal protein L20"
FT                   /id="PRO_0000177109"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:2GHJ"
FT   HELIX           28..68
FT                   /evidence="ECO:0007829|PDB:2GHJ"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:2GHJ"
FT   HELIX           74..81
FT                   /evidence="ECO:0007829|PDB:2GHJ"
FT   TURN            82..85
FT                   /evidence="ECO:0007829|PDB:2GHJ"
FT   HELIX           90..99
FT                   /evidence="ECO:0007829|PDB:2GHJ"
FT   HELIX           101..115
FT                   /evidence="ECO:0007829|PDB:2GHJ"
SQ   SEQUENCE   118 AA;  14004 MW;  5CDF2BD818933C00 CRC64;
     MRVKGPSSRR KKKKILKLAK GYRGQRSRSY RRAKEAVMRA LYYQYRDRKL RKREFRRLWI
     ARINAAVRAY GLNYSTFING LKKAGIELDR KILADMAVRD PQAFEQVVNK VKEALQVQ