ID   RL6_DEIRA               Reviewed;         185 AA.
AC   Q9RSL3;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Large ribosomal subunit protein uL6 {ECO:0000255|HAMAP-Rule:MF_01365};
DE   AltName: Full=50S ribosomal protein L6 {ECO:0000305};
GN   Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365};
GN   OrderedLocusNames=DR_2111;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS   27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC   Bacteria; Deinococcota; 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 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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: It is located near the subunit interface in the base of the
CC       L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase
CC       center (By similarity). This protein binds to the 23S rRNA, and is
CC       important in its secondary structure. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01365, 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 universal ribosomal protein uL6 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01365}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF11660.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000513; AAF11660.1; ALT_INIT; Genomic_DNA.
DR   PIR; B75314; B75314.
DR   RefSeq; NP_295834.2; NC_001263.1.
DR   RefSeq; WP_010888742.1; NZ_JMLF01000004.1.
DR   PDB; 1NKW; X-ray; 3.10 A; E=1-185.
DR   PDB; 1NWX; X-ray; 3.50 A; E=1-185.
DR   PDB; 1NWY; X-ray; 3.30 A; E=1-185.
DR   PDB; 1SM1; X-ray; 3.42 A; E=1-185.
DR   PDB; 1XBP; X-ray; 3.50 A; E=1-185.
DR   PDB; 2ZJP; X-ray; 3.70 A; E=1-185.
DR   PDB; 2ZJQ; X-ray; 3.30 A; E=1-185.
DR   PDB; 2ZJR; X-ray; 2.91 A; E=1-185.
DR   PDB; 3CF5; X-ray; 3.30 A; E=1-185.
DR   PDB; 3DLL; X-ray; 3.50 A; E=1-185.
DR   PDB; 3PIO; X-ray; 3.25 A; E=1-185.
DR   PDB; 3PIP; X-ray; 3.45 A; E=1-185.
DR   PDB; 4IO9; X-ray; 3.20 A; E=1-185.
DR   PDB; 4IOA; X-ray; 3.20 A; E=1-185.
DR   PDB; 4IOC; X-ray; 3.60 A; E=1-185.
DR   PDB; 4U67; X-ray; 3.65 A; E=1-185.
DR   PDB; 4V49; X-ray; 8.70 A; E=5-181.
DR   PDB; 4V4A; X-ray; 9.50 A; E=5-181.
DR   PDB; 4V4G; X-ray; 11.50 A; H=5-181.
DR   PDB; 4WFN; X-ray; 3.54 A; E=1-185.
DR   PDB; 5DM6; X-ray; 2.90 A; E=5-175.
DR   PDB; 5DM7; X-ray; 3.00 A; E=5-175.
DR   PDB; 5JVG; X-ray; 3.43 A; E=1-185.
DR   PDB; 5JVH; X-ray; 3.58 A; E=1-185.
DR   PDB; 7A0R; X-ray; 3.30 A; E=5-175.
DR   PDB; 7A0S; X-ray; 3.22 A; E=5-175.
DR   PDB; 7A18; X-ray; 3.40 A; E=5-175.
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; Q9RSL3; -.
DR   SMR; Q9RSL3; -.
DR   IntAct; Q9RSL3; 1.
DR   STRING; 243230.DR_2111; -.
DR   PaxDb; 243230-DR_2111; -.
DR   EnsemblBacteria; AAF11660; AAF11660; DR_2111.
DR   GeneID; 69518353; -.
DR   KEGG; dra:DR_2111; -.
DR   PATRIC; fig|243230.17.peg.2334; -.
DR   eggNOG; COG0097; Bacteria.
DR   HOGENOM; CLU_065464_1_2_0; -.
DR   InParanoid; Q9RSL3; -.
DR   OrthoDB; 9805007at2; -.
DR   EvolutionaryTrace; Q9RSL3; -.
DR   Proteomes; UP000002524; Chromosome I.
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:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR   Gene3D; 3.90.930.12; Ribosomal protein L6, alpha-beta domain; 2.
DR   HAMAP; MF_01365_B; Ribosomal_uL6_B; 1.
DR   InterPro; IPR000702; Ribosomal_uL6-like.
DR   InterPro; IPR036789; Ribosomal_uL6-like_a/b-dom_sf.
DR   InterPro; IPR020040; Ribosomal_uL6_a/b-dom.
DR   InterPro; IPR019906; Ribosomal_uL6_bac-type.
DR   NCBIfam; TIGR03654; L6_bact; 1.
DR   PANTHER; PTHR11655:SF14; 54S RIBOSOMAL PROTEIN L6, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11655; 60S/50S RIBOSOMAL PROTEIN L6/L9; 1.
DR   Pfam; PF00347; Ribosomal_L6; 2.
DR   PIRSF; PIRSF002162; Ribosomal_L6; 1.
DR   PRINTS; PR00059; RIBOSOMALL6.
DR   SUPFAM; SSF56053; Ribosomal protein L6; 2.
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..185
FT                   /note="Large ribosomal subunit protein uL6"
FT                   /id="PRO_0000131047"
FT   STRAND          16..18
FT                   /evidence="ECO:0007829|PDB:4IO9"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:7A0R"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:4IO9"
FT   STRAND          33..36
FT                   /evidence="ECO:0007829|PDB:3PIO"
FT   STRAND          39..41
FT                   /evidence="ECO:0007829|PDB:2ZJR"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          47..52
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:3PIO"
FT   HELIX           60..79
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          83..91
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:4IO9"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:4IO9"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          121..124
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          130..136
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           138..150
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          161..164
FT                   /evidence="ECO:0007829|PDB:5DM6"
SQ   SEQUENCE   185 AA;  19582 MW;  00E39D11826B4C1D CRC64;
     MSRIGKQPIA VPSGVTVNAQ DGVFKVKGPK GELTVPYNTE LTVRQDGDQL LVERPSDAQK
     HRALHGLTRT LVANAVKGVS DGYTINLELR GVGFRAKLTG KALEMNIGYS HPVIIEPPAG
     VTFAVPEPTR IDVSGIDKQL VGQVAANVRK VRKPDAYHGK GVRFVGEQIA LKAGKAGATG
     GKGKK
//