RL21_BACSU
ID RL21_BACSU Reviewed; 102 AA.
AC P26908;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=50S ribosomal protein L21 {ECO:0000255|HAMAP-Rule:MF_01363};
DE AltName: Full=BL20;
GN Name=rplU {ECO:0000255|HAMAP-Rule:MF_01363}; OrderedLocusNames=BSU27960;
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=1942049; DOI=10.1016/0022-2836(91)90931-u;
RA Cutting S.M., Roels S., Losick R.;
RT "Sporulation operon spoIVF and the characterization of mutations that
RT uncouple mother-cell from forespore gene expression in Bacillus subtilis.";
RL J. Mol. Biol. 221:1237-1256(1991).
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 1-102 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: This protein binds to 23S rRNA in the presence of protein
CC L20. {ECO:0000255|HAMAP-Rule:MF_01363}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:30126986). Contacts
CC protein L20 (By similarity). {ECO:0000255|HAMAP-Rule:MF_01363,
CC ECO:0000269|PubMed:30126986}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family.
CC {ECO:0000255|HAMAP-Rule:MF_01363}.
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; X59528; CAA42108.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14756.1; -; Genomic_DNA.
DR PIR; S18439; S18439.
DR RefSeq; NP_390674.1; NC_000964.3.
DR RefSeq; WP_003229668.1; NZ_JNCM01000036.1.
DR PDB; 3J3V; EM; 13.30 A; R=1-102.
DR PDB; 3J3W; EM; 10.70 A; R=1-102.
DR PDB; 3J9W; EM; 3.90 A; BU=1-102.
DR PDB; 5NJT; EM; 3.80 A; k=2-102.
DR PDB; 6HA1; EM; 3.10 A; R=1-102.
DR PDB; 6HA8; EM; 3.50 A; R=1-102.
DR PDB; 6HTQ; EM; 4.50 A; R=2-102.
DR PDB; 6PPF; EM; 3.40 A; R=1-102.
DR PDB; 6PPK; EM; 4.40 A; R=1-102.
DR PDB; 6PVK; EM; 3.40 A; R=1-102.
DR PDB; 6TNN; EM; 3.07 A; k=1-102.
DR PDB; 6TPQ; EM; 3.07 A; k=1-102.
DR PDB; 7AQC; EM; 2.99 A; g=1-102.
DR PDB; 7AQD; EM; 3.10 A; g=1-102.
DR PDB; 7AS8; EM; 2.90 A; V=1-102.
DR PDB; 7AS9; EM; 3.50 A; V=1-102.
DR PDB; 7O5B; EM; 3.33 A; o=1-102.
DR PDB; 7OPE; EM; 3.20 A; V=1-102.
DR PDB; 7QV1; EM; 3.50 A; R=1-102.
DR PDB; 7QV2; EM; 3.50 A; R=1-102.
DR PDB; 7QV3; EM; 5.14 A; R=1-102.
DR PDB; 7SAE; EM; 3.00 A; R=1-102.
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; 7SAE; -.
DR AlphaFoldDB; P26908; -.
DR SMR; P26908; -.
DR IntAct; P26908; 1.
DR STRING; 224308.BSU27960; -.
DR jPOST; P26908; -.
DR PaxDb; P26908; -.
DR PRIDE; P26908; -.
DR EnsemblBacteria; CAB14756; CAB14756; BSU_27960.
DR GeneID; 936368; -.
DR KEGG; bsu:BSU27960; -.
DR PATRIC; fig|224308.179.peg.3038; -.
DR eggNOG; COG0261; Bacteria.
DR InParanoid; P26908; -.
DR OMA; HRQEITR; -.
DR PhylomeDB; P26908; -.
DR BioCyc; BSUB:BSU27960-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01363; Ribosomal_L21; 1.
DR InterPro; IPR036164; L21-like_sf.
DR InterPro; IPR028909; L21p-like.
DR InterPro; IPR001787; Ribosomal_L21.
DR InterPro; IPR018258; Ribosomal_L21_CS.
DR PANTHER; PTHR21349; PTHR21349; 1.
DR Pfam; PF00829; Ribosomal_L21p; 1.
DR SUPFAM; SSF141091; SSF141091; 1.
DR TIGRFAMs; TIGR00061; L21; 1.
DR PROSITE; PS01169; RIBOSOMAL_L21; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..102
FT /note="50S ribosomal protein L21"
FT /id="PRO_0000180990"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:7AQC"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:7AS8"
SQ SEQUENCE 102 AA; 11275 MW; EEBCFDDFD5FEFEDC CRC64;
MYAIIKTGGK QIKVEEGQTV YIEKLAAEAG ETVTFEDVLF VGGDNVKVGN PTVEGATVTA
KVEKQGRAKK ITVFRYKPKK NVHKKQGHRQ PYTKVTIEKI NA
