RL20_BACSU
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 03-AUG-2022, entry version 128.
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 PDB; 7O5B; EM; 3.33 A; n=1-119.
DR PDB; 7OPE; EM; 3.20 A; U=1-119.
DR PDB; 7QV1; EM; 3.50 A; Q=1-119.
DR PDB; 7QV2; EM; 3.50 A; Q=1-119.
DR PDB; 7QV3; EM; 5.14 A; Q=1-119.
DR PDB; 7S9U; EM; 3.20 A; Q=1-119.
DR PDB; 7SAE; EM; 3.00 A; Q=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 PDBsum; 7O5B; -.
DR PDBsum; 7OPE; -.
DR PDBsum; 7QV1; -.
DR PDBsum; 7QV2; -.
DR PDBsum; 7QV3; -.
DR PDBsum; 7S9U; -.
DR PDBsum; 7SAE; -.
DR AlphaFoldDB; P55873; -.
DR SMR; P55873; -.
DR IntAct; P55873; 1.
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-MON; -.
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
