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Database: UniProt
Entry: P55873
LinkDB: P55873
Original site: P55873 
ID   RL20_BACSU              Reviewed;         119 AA.
AC   P55873;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   29-SEP-2021, entry version 125.
DE   RecName: Full=50S ribosomal protein L20;
GN   Name=rplT; OrderedLocusNames=BSU28850;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-119 WITH AND WITHOUT
RP   VIRGINIAMYCIN M, AND SUBUNIT.
RX   PubMed=30126986; DOI=10.1073/pnas.1808535115;
RA   Crowe-McAuliffe C., Graf M., Huter P., Takada H., Abdelshahid M.,
RA   Novacek J., Murina V., Atkinson G.C., Hauryliuk V., Wilson D.N.;
RT   "Structural basis for antibiotic resistance mediated by the Bacillus
RT   subtilis ABCF ATPase VmlR.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:8978-8983(2018).
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   -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC       {ECO:0000269|PubMed:30126986}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family.
CC       {ECO:0000305}.
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DR   EMBL; Z75208; CAA99618.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14845.1; -; Genomic_DNA.
DR   PIR; F69696; F69696.
DR   RefSeq; NP_390763.1; NC_000964.3.
DR   RefSeq; WP_003222420.1; NZ_JNCM01000036.1.
DR   PDB; 3J3V; EM; 13.30 A; Q=1-119.
DR   PDB; 3J3W; EM; 10.70 A; Q=1-119.
DR   PDB; 3J9W; EM; 3.90 A; BT=1-119.
DR   PDB; 5NJT; EM; 3.80 A; j=2-118.
DR   PDB; 6HA1; EM; 3.10 A; Q=1-119.
DR   PDB; 6HA8; EM; 3.50 A; Q=1-119.
DR   PDB; 6HTQ; EM; 4.50 A; Q=2-118.
DR   PDB; 6PPF; EM; 3.40 A; Q=2-119.
DR   PDB; 6PPK; EM; 4.40 A; Q=2-119.
DR   PDB; 6PVK; EM; 3.40 A; Q=2-119.
DR   PDB; 6TNN; EM; 3.07 A; j=1-119.
DR   PDB; 6TPQ; EM; 3.07 A; j=1-119.
DR   PDB; 7AQC; EM; 2.99 A; Q=1-119.
DR   PDB; 7AQD; EM; 3.10 A; Q=1-119.
DR   PDB; 7AS8; EM; 2.90 A; U=1-119.
DR   PDB; 7AS9; EM; 3.50 A; U=1-119.
DR   PDBsum; 3J3V; -.
DR   PDBsum; 3J3W; -.
DR   PDBsum; 3J9W; -.
DR   PDBsum; 5NJT; -.
DR   PDBsum; 6HA1; -.
DR   PDBsum; 6HA8; -.
DR   PDBsum; 6HTQ; -.
DR   PDBsum; 6PPF; -.
DR   PDBsum; 6PPK; -.
DR   PDBsum; 6PVK; -.
DR   PDBsum; 6TNN; -.
DR   PDBsum; 6TPQ; -.
DR   PDBsum; 7AQC; -.
DR   PDBsum; 7AQD; -.
DR   PDBsum; 7AS8; -.
DR   PDBsum; 7AS9; -.
DR   SMR; P55873; -.
DR   STRING; 224308.BSU28850; -.
DR   jPOST; P55873; -.
DR   PaxDb; P55873; -.
DR   PRIDE; P55873; -.
DR   DNASU; 936645; -.
DR   EnsemblBacteria; CAB14845; CAB14845; BSU_28850.
DR   GeneID; 50136652; -.
DR   GeneID; 64304615; -.
DR   GeneID; 936645; -.
DR   KEGG; bsu:BSU28850; -.
DR   PATRIC; fig|224308.179.peg.3133; -.
DR   eggNOG; COG0292; Bacteria.
DR   InParanoid; P55873; -.
DR   OMA; GRRKNVW; -.
DR   PhylomeDB; P55873; -.
DR   BioCyc; BSUB:BSU28850-MONOMER; -.
DR   Proteomes; UP000001570; 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   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..119
FT                   /note="50S ribosomal protein L20"
FT                   /id="PRO_0000177120"
FT   HELIX           8..20
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   TURN            21..23
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   HELIX           27..30
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   HELIX           32..72
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   HELIX           76..86
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   HELIX           92..100
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   HELIX           103..116
FT                   /evidence="ECO:0007829|PDB:7AS8"
SQ   SEQUENCE   119 AA;  13638 MW;  DC93F0CDC9D5E606 CRC64;
     MPRVKGGTVT RKRRKKVLKL AKGYFGSKHT LYKVANQQVM KSGNYAFRDR RQKKRDFRKL
     WITRINAAAR MNGLSYSRLM HGLKLSGIEV NRKMLADLAV NDLTAFNQLA DAAKAQLNK
//
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