ID   RL20_ACIB5              Reviewed;         119 AA.
AC   B7I694;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=50S ribosomal protein L20 {ECO:0000255|HAMAP-Rule:MF_00382};
GN   Name=rplT {ECO:0000255|HAMAP-Rule:MF_00382}; OrderedLocusNames=AB57_0701;
OS   Acinetobacter baumannii (strain AB0057).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=480119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB0057;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(2008).
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}.
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DR   EMBL; CP001182; ACJ40121.1; -; Genomic_DNA.
DR   RefSeq; WP_000124858.1; NC_011586.2.
DR   PDB; 7M4V; EM; 2.54 A; P=1-119.
DR   PDBsum; 7M4V; -.
DR   AlphaFoldDB; B7I694; -.
DR   SMR; B7I694; -.
DR   IntAct; B7I694; 2.
DR   GeneID; 67513207; -.
DR   KEGG; abn:AB57_0701; -.
DR   HOGENOM; CLU_123265_0_1_6; -.
DR   OMA; GRRKNVW; -.
DR   Proteomes; UP000007094; 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   1: Evidence at protein level;
KW   3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..119
FT                   /note="50S ribosomal protein L20"
FT                   /id="PRO_1000122256"
FT   HELIX           7..20
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   TURN            21..23
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           26..29
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           32..71
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           76..86
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           92..101
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           103..117
FT                   /evidence="ECO:0007829|PDB:7M4V"
SQ   SEQUENCE   119 AA;  13437 MW;  F8C03ED66CFDAFF2 CRC64;
     MARVKRGVVA HRRHKKILAR AKGYYGARSR VYRVAFQAVI KAGQYAYRDR RQKKRQFRAL
     WIARINAGAR QNGLSYSRMI DGLKKAQVII DRRVLADIAM HDAVAFAALA EKAKGALAA