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RL18_DEIRA
ID   RL18_DEIRA              Reviewed;         114 AA.
AC   Q9RSL2;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=50S ribosomal protein L18;
GN   Name=rplR; OrderedLocusNames=DR_2112;
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 1-6.
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: This is one of the proteins that binds and mediates the
CC       attachment of the 5S RNA into the large ribosomal subunit, where it
CC       forms part of the central protuberance.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC       rRNA/L5/L18/L25 subcomplex. Contacts the 23S rRNA (By similarity).
CC       Contacts protein L27 and the 5S rRNA. {ECO:0000250,
CC       ECO:0000269|PubMed:11677599, ECO:0000269|PubMed:12535524,
CC       ECO:0000269|PubMed:12623020, ECO:0000269|PubMed:12665853,
CC       ECO:0000269|PubMed:15059283, ECO:0000269|PubMed:15554968}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000305}.
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DR   EMBL; AE000513; AAF11661.1; -; Genomic_DNA.
DR   PIR; C75314; C75314.
DR   RefSeq; NP_295835.1; NC_001263.1.
DR   RefSeq; WP_010888743.1; NZ_CP015081.1.
DR   PDB; 1NKW; X-ray; 3.10 A; M=1-114.
DR   PDB; 1NWX; X-ray; 3.50 A; M=2-114.
DR   PDB; 1NWY; X-ray; 3.30 A; M=2-114.
DR   PDB; 1SM1; X-ray; 3.42 A; M=1-114.
DR   PDB; 1XBP; X-ray; 3.50 A; M=2-114.
DR   PDB; 2ZJP; X-ray; 3.70 A; L=1-114.
DR   PDB; 2ZJQ; X-ray; 3.30 A; L=1-114.
DR   PDB; 2ZJR; X-ray; 2.91 A; L=1-114.
DR   PDB; 3CF5; X-ray; 3.30 A; L=1-114.
DR   PDB; 3DLL; X-ray; 3.50 A; L=1-114.
DR   PDB; 3PIO; X-ray; 3.25 A; L=1-114.
DR   PDB; 3PIP; X-ray; 3.45 A; L=1-114.
DR   PDB; 4IO9; X-ray; 3.20 A; L=1-114.
DR   PDB; 4IOA; X-ray; 3.20 A; L=1-114.
DR   PDB; 4IOC; X-ray; 3.60 A; L=1-114.
DR   PDB; 4U67; X-ray; 3.65 A; L=1-114.
DR   PDB; 4V49; X-ray; 8.70 A; M=4-114.
DR   PDB; 4V4A; X-ray; 9.50 A; M=4-114.
DR   PDB; 4V4G; X-ray; 11.50 A; P=4-114.
DR   PDB; 4WFN; X-ray; 3.54 A; L=1-114.
DR   PDB; 5DM6; X-ray; 2.90 A; L=8-111.
DR   PDB; 5DM7; X-ray; 3.00 A; L=8-111.
DR   PDB; 5JVG; X-ray; 3.43 A; L=1-114.
DR   PDB; 5JVH; X-ray; 3.58 A; L=1-114.
DR   PDB; 7A0R; X-ray; 3.30 A; L=8-111.
DR   PDB; 7A0S; X-ray; 3.22 A; L=8-111.
DR   PDB; 7A18; X-ray; 3.40 A; L=8-111.
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; 4WFN; -.
DR   PDBsum; 5DM6; -.
DR   PDBsum; 5DM7; -.
DR   PDBsum; 5JVG; -.
DR   PDBsum; 5JVH; -.
DR   PDBsum; 7A0R; -.
DR   PDBsum; 7A0S; -.
DR   PDBsum; 7A18; -.
DR   AlphaFoldDB; Q9RSL2; -.
DR   SMR; Q9RSL2; -.
DR   IntAct; Q9RSL2; 1.
DR   STRING; 243230.DR_2112; -.
DR   EnsemblBacteria; AAF11661; AAF11661; DR_2112.
DR   KEGG; dra:DR_2112; -.
DR   PATRIC; fig|243230.17.peg.2335; -.
DR   eggNOG; COG0256; Bacteria.
DR   HOGENOM; CLU_098841_0_1_0; -.
DR   InParanoid; Q9RSL2; -.
DR   OMA; NKQIYAQ; -.
DR   OrthoDB; 1963491at2; -.
DR   EvolutionaryTrace; Q9RSL2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0008097; F:5S rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01337_B; Ribosomal_L18_B; 1.
DR   InterPro; IPR005484; Ribosomal_L18.
DR   InterPro; IPR004389; Ribosomal_L18_bac-type.
DR   PANTHER; PTHR12899; PTHR12899; 1.
DR   Pfam; PF00861; Ribosomal_L18p; 1.
DR   TIGRFAMs; TIGR00060; L18_bact; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..114
FT                   /note="50S ribosomal protein L18"
FT                   /id="PRO_0000131255"
FT   HELIX           10..18
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   TURN            22..24
FT                   /evidence="ECO:0007829|PDB:2ZJR"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:2ZJR"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:5DM7"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   TURN            45..48
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:5DM7"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:2ZJR"
FT   HELIX           68..82
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:4IO9"
FT   STRAND          96..98
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           99..109
FT                   /evidence="ECO:0007829|PDB:5DM6"
SQ   SEQUENCE   114 AA;  12139 MW;  35010FFD7FE00A55 CRC64;
     MATATTIRRK LRTRRKVRTT TAASGRLRLS VYRSSKHIYA QIIDDSRGQT LAAASSAALK
     SGNKTDTAAA VGKALAAAAA EKGIKQVVFD RGSYKYHGRV KALADAAREG GLDF
 
 
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