RL21_DEIRA
ID RL21_DEIRA Reviewed; 100 AA.
AC Q9RY64;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=50S ribosomal protein L21 {ECO:0000255|HAMAP-Rule:MF_01363};
GN Name=rplU {ECO:0000255|HAMAP-Rule:MF_01363}; OrderedLocusNames=DR_0086;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT, AND PROTEIN
RP SEQUENCE OF 1-5.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=11733066; DOI=10.1016/s0092-8674(01)00546-3;
RA Harms J., Schluenzen F., Zarivach R., Bashan A., Gat S., Agmon I.,
RA Bartels H., Franceschi F., Yonath A.;
RT "High resolution structure of the large ribosomal subunit from a mesophilic
RT eubacterium.";
RL Cell 107:679-688(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP FIVE ANTIBIOTICS.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=11677599; DOI=10.1038/35101544;
RA Schluenzen F., Zarivach R., Harms J., Bashan A., Tocilj A., Albrecht R.,
RA Yonath A., Franceschi F.;
RT "Structural basis for the interaction of antibiotics with the peptidyl
RT transferase centre in eubacteria.";
RL Nature 413:814-821(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP TRNA MIMICS.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=12535524; DOI=10.1016/s1097-2765(03)00009-1;
RA Bashan A., Agmon I., Zarivach R., Schluenzen F., Harms J., Berisio R.,
RA Bartels H., Franceschi F., Auerbach T., Hansen H.A., Kossoy E., Kessler M.,
RA Yonath A.;
RT "Structural basis of the ribosomal machinery for peptide bond formation,
RT translocation, and nascent chain progression.";
RL Mol. Cell 11:91-102(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP MODIFIED MACROLIDE ANTIBIOTICS.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=12623020; DOI=10.1016/s0969-2126(03)00022-4;
RA Schluenzen F., Harms J.M., Franceschi F., Hansen H.A., Bartels H.,
RA Zarivach R., Yonath A.;
RT "Structural basis for the antibiotic activity of ketolides and azalides.";
RL Structure 11:329-338(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP TROLEANDOMYCIN.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=12665853; DOI=10.1038/nsb915;
RA Berisio R., Schluenzen F., Harms J., Bashan A., Auerbach T., Baram D.,
RA Yonath A.;
RT "Structural insight into the role of the ribosomal tunnel in cellular
RT regulation.";
RL Nat. Struct. Biol. 10:366-370(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP THE STREPTOGRAMINS QUINUPRISTIN AND DALFOPRISTIN.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15059283; DOI=10.1186/1741-7007-2-4;
RA Harms J.M., Schluenzen F., Fucini P., Bartels H., Yonath A.;
RT "Alterations at the peptidyl transferase centre of the ribosome induced by
RT the synergistic action of the streptogramins dalfopristin and
RT quinupristin.";
RL BMC Biol. 2:4-4(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP TIAMULIN.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15554968; DOI=10.1111/j.1365-2958.2004.04346.x;
RA Schluenzen F., Pyetan E., Fucini P., Yonath A., Harms J.M.;
RT "Inhibition of peptide bond formation by pleuromutilins: the structure of
RT the 50S ribosomal subunit from Deinococcus radiodurans in complex with
RT tiamulin.";
RL Mol. Microbiol. 54:1287-1294(2004).
CC -!- FUNCTION: Binds directly to 23S rRNA, probably serving to organize its
CC structure.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts proteins L15 and
CC L20. {ECO:0000255|HAMAP-Rule:MF_01363, ECO:0000269|PubMed:11677599,
CC ECO:0000269|PubMed:12535524, ECO:0000269|PubMed:12623020,
CC ECO:0000269|PubMed:12665853, ECO:0000269|PubMed:15059283,
CC ECO:0000269|PubMed:15554968}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family.
CC {ECO:0000255|HAMAP-Rule:MF_01363}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF09679.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000513; AAF09679.1; ALT_INIT; Genomic_DNA.
DR PIR; F75560; F75560.
DR RefSeq; NP_293812.1; NC_001263.1.
DR RefSeq; WP_027480310.1; NZ_CP015081.1.
DR PDB; 1NKW; X-ray; 3.10 A; P=1-100.
DR PDB; 1NWX; X-ray; 3.50 A; P=1-100.
DR PDB; 1NWY; X-ray; 3.30 A; P=1-100.
DR PDB; 1SM1; X-ray; 3.42 A; P=1-100.
DR PDB; 1XBP; X-ray; 3.50 A; P=1-100.
DR PDB; 2ZJP; X-ray; 3.70 A; O=1-100.
DR PDB; 2ZJQ; X-ray; 3.30 A; O=1-100.
DR PDB; 2ZJR; X-ray; 2.91 A; O=1-100.
DR PDB; 3CF5; X-ray; 3.30 A; O=1-100.
DR PDB; 3DLL; X-ray; 3.50 A; O=1-100.
DR PDB; 3PIO; X-ray; 3.25 A; O=1-100.
DR PDB; 3PIP; X-ray; 3.45 A; O=1-100.
DR PDB; 4IO9; X-ray; 3.20 A; O=1-100.
DR PDB; 4IOA; X-ray; 3.20 A; O=1-100.
DR PDB; 4IOC; X-ray; 3.60 A; O=1-100.
DR PDB; 4U67; X-ray; 3.65 A; O=1-100.
DR PDB; 4V49; X-ray; 8.70 A; P=1-100.
DR PDB; 4V4A; X-ray; 9.50 A; P=1-100.
DR PDB; 4V4G; X-ray; 11.50 A; S=1-100.
DR PDB; 4V4R; X-ray; 5.90 A; BV=1-100.
DR PDB; 4V4S; X-ray; 6.76 A; BV=1-100.
DR PDB; 4V4T; X-ray; 6.46 A; V=1-100.
DR PDB; 4WFN; X-ray; 3.54 A; O=1-100.
DR PDB; 5DM6; X-ray; 2.90 A; O=5-98.
DR PDB; 5DM7; X-ray; 3.00 A; O=5-98.
DR PDB; 5JVG; X-ray; 3.43 A; O=1-100.
DR PDB; 5JVH; X-ray; 3.58 A; O=1-100.
DR PDB; 7A0R; X-ray; 3.30 A; O=1-98.
DR PDB; 7A0S; X-ray; 3.22 A; O=1-98.
DR PDB; 7A18; X-ray; 3.40 A; O=1-98.
DR PDBsum; 1NKW; -.
DR PDBsum; 1NWX; -.
DR PDBsum; 1NWY; -.
DR PDBsum; 1SM1; -.
DR PDBsum; 1XBP; -.
DR PDBsum; 2ZJP; -.
DR PDBsum; 2ZJQ; -.
DR PDBsum; 2ZJR; -.
DR PDBsum; 3CF5; -.
DR PDBsum; 3DLL; -.
DR PDBsum; 3PIO; -.
DR PDBsum; 3PIP; -.
DR PDBsum; 4IO9; -.
DR PDBsum; 4IOA; -.
DR PDBsum; 4IOC; -.
DR PDBsum; 4U67; -.
DR PDBsum; 4V49; -.
DR PDBsum; 4V4A; -.
DR PDBsum; 4V4G; -.
DR PDBsum; 4V4R; -.
DR PDBsum; 4V4S; -.
DR PDBsum; 4V4T; -.
DR PDBsum; 4WFN; -.
DR PDBsum; 5DM6; -.
DR PDBsum; 5DM7; -.
DR PDBsum; 5JVG; -.
DR PDBsum; 5JVH; -.
DR PDBsum; 7A0R; -.
DR PDBsum; 7A0S; -.
DR PDBsum; 7A18; -.
DR AlphaFoldDB; Q9RY64; -.
DR SMR; Q9RY64; -.
DR IntAct; Q9RY64; 1.
DR STRING; 243230.DR_0086; -.
DR EnsemblBacteria; AAF09679; AAF09679; DR_0086.
DR KEGG; dra:DR_0086; -.
DR PATRIC; fig|243230.17.peg.250; -.
DR eggNOG; COG0261; Bacteria.
DR HOGENOM; CLU_1575895_0_0_0; -.
DR InParanoid; Q9RY64; -.
DR OMA; HRQEITR; -.
DR OrthoDB; 1949059at2; -.
DR EvolutionaryTrace; Q9RY64; -.
DR Proteomes; UP000002524; Chromosome I.
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 PANTHER; PTHR21349; PTHR21349; 1.
DR Pfam; PF00829; Ribosomal_L21p; 1.
DR SUPFAM; SSF141091; SSF141091; 1.
DR TIGRFAMs; TIGR00061; L21; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..100
FT /note="50S ribosomal protein L21"
FT /id="PRO_0000180999"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:5JVG"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:7A18"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5DM7"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:4IO9"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 54..65
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:5DM6"
SQ SEQUENCE 100 AA; 11147 MW; 98F6DEFE41810D1F CRC64;
MFAIIQTGGK QYRVSEGDVI RVESLQGEAG DKVELKALFV GGEQTVFGED AGKYTVQAEV
VEHGRGKKIY IRKYKSGVQY RRRTGHRQNF TAIKILGIQG
