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RL17_DEIRA
ID   RL17_DEIRA              Reviewed;         116 AA.
AC   Q9RSJ5;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=50S ribosomal protein L17 {ECO:0000255|HAMAP-Rule:MF_01368};
GN   Name=rplQ {ECO:0000255|HAMAP-Rule:MF_01368}; OrderedLocusNames=DR_2129;
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, PROTEIN SEQUENCE
RP   OF 1-5, AND CONTACTS WITH 23S RRNA.
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 to the 23S rRNA.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts proteins L3 and
CC       L32. {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 bacterial ribosomal protein bL17 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01368}.
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DR   EMBL; AE000513; AAF11679.1; -; Genomic_DNA.
DR   PIR; B75313; B75313.
DR   RefSeq; NP_295852.1; NC_001263.1.
DR   RefSeq; WP_010888760.1; NZ_CP015081.1.
DR   PDB; 1NKW; X-ray; 3.10 A; L=1-116.
DR   PDB; 1NWX; X-ray; 3.50 A; L=1-116.
DR   PDB; 1NWY; X-ray; 3.30 A; L=1-116.
DR   PDB; 1SM1; X-ray; 3.42 A; L=1-116.
DR   PDB; 1XBP; X-ray; 3.50 A; L=1-116.
DR   PDB; 2ZJP; X-ray; 3.70 A; K=1-116.
DR   PDB; 2ZJQ; X-ray; 3.30 A; K=1-116.
DR   PDB; 2ZJR; X-ray; 2.91 A; K=1-116.
DR   PDB; 3CF5; X-ray; 3.30 A; K=1-116.
DR   PDB; 3DLL; X-ray; 3.50 A; K=1-116.
DR   PDB; 3PIO; X-ray; 3.25 A; K=1-116.
DR   PDB; 3PIP; X-ray; 3.45 A; K=1-116.
DR   PDB; 4IO9; X-ray; 3.20 A; K=1-116.
DR   PDB; 4IOA; X-ray; 3.20 A; K=1-116.
DR   PDB; 4IOC; X-ray; 3.60 A; K=1-116.
DR   PDB; 4U67; X-ray; 3.65 A; K=1-116.
DR   PDB; 4V49; X-ray; 8.70 A; L=3-116.
DR   PDB; 4V4A; X-ray; 9.50 A; L=3-116.
DR   PDB; 4V4G; X-ray; 11.50 A; O=3-116.
DR   PDB; 4WFN; X-ray; 3.54 A; K=1-116.
DR   PDB; 5DM6; X-ray; 2.90 A; K=3-115.
DR   PDB; 5DM7; X-ray; 3.00 A; K=3-115.
DR   PDB; 5JVG; X-ray; 3.43 A; K=1-116.
DR   PDB; 5JVH; X-ray; 3.58 A; K=1-116.
DR   PDB; 7A0R; X-ray; 3.30 A; K=1-116.
DR   PDB; 7A0S; X-ray; 3.22 A; K=1-116.
DR   PDB; 7A18; X-ray; 3.40 A; K=1-115.
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; Q9RSJ5; -.
DR   SMR; Q9RSJ5; -.
DR   IntAct; Q9RSJ5; 1.
DR   STRING; 243230.DR_2129; -.
DR   EnsemblBacteria; AAF11679; AAF11679; DR_2129.
DR   KEGG; dra:DR_2129; -.
DR   PATRIC; fig|243230.17.peg.2352; -.
DR   eggNOG; COG0203; Bacteria.
DR   HOGENOM; CLU_074407_2_0_0; -.
DR   InParanoid; Q9RSJ5; -.
DR   OMA; YAVTELF; -.
DR   OrthoDB; 1838961at2; -.
DR   EvolutionaryTrace; Q9RSJ5; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1030.10; -; 1.
DR   HAMAP; MF_01368; Ribosomal_L17; 1.
DR   InterPro; IPR000456; Ribosomal_L17.
DR   InterPro; IPR036373; Ribosomal_L17_sf.
DR   PANTHER; PTHR14413; PTHR14413; 1.
DR   Pfam; PF01196; Ribosomal_L17; 1.
DR   SUPFAM; SSF64263; SSF64263; 1.
DR   TIGRFAMs; TIGR00059; L17; 1.
DR   PROSITE; PS01167; RIBOSOMAL_L17; 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..116
FT                   /note="50S ribosomal protein L17"
FT                   /id="PRO_0000175523"
FT   HELIX           14..30
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           38..55
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           60..69
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           73..81
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           83..87
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:3PIO"
FT   STRAND          96..102
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          109..114
FT                   /evidence="ECO:0007829|PDB:5DM6"
SQ   SEQUENCE   116 AA;  12899 MW;  FF09A10C397D7D9C CRC64;
     MRHGKAGRKL NRNSSARVAL ARAQATALLR EGRIQTTLTK AKELRPFVEQ LITTAKGGDL
     HSRRLVAQDI HDKDVVRKVM DEVAPKYAER PGGYTRILRV GTRRGDGVTM ALIELV
 
 
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