ID   RL20_CUTAK              Reviewed;         123 AA.
AC   Q6A7V3;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=50S ribosomal protein L20 {ECO:0000255|HAMAP-Rule:MF_00382};
GN   Name=rplT {ECO:0000255|HAMAP-Rule:MF_00382}; OrderedLocusNames=PPA1412;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00382}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00382}.
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; AE017283; AAT83162.1; -; Genomic_DNA.
DR   RefSeq; WP_002514221.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6A7V3; -.
DR   SMR; Q6A7V3; -.
DR   STRING; 267747.PPA1412; -.
DR   EnsemblBacteria; AAT83162; AAT83162; PPA1412.
DR   KEGG; pac:PPA1412; -.
DR   eggNOG; COG0292; Bacteria.
DR   HOGENOM; CLU_123265_0_0_11; -.
DR   OMA; GRRKNVW; -.
DR   Proteomes; UP000000603; Chromosome.
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:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd07026; Ribosomal_L20; 1.
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   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..123
FT                   /note="50S ribosomal protein L20"
FT                   /id="PRO_0000177202"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   123 AA;  13987 MW;  A4EE019F6B0E8316 CRC64;
     MARVKRSVNA KKKRREVLDQ ASGYRGQRSR LYRKAKEQTL HSATYSFRDR RAKKGDFRSL
     WIQRINAASR AQGMTYNRFI NGLKNAGVEV DRKMLAELAV SDINAFNSLV EVAKANQPQN
     AAA