RL6_DEIRA
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 25-MAY-2022, entry version 128.
DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365};
GN Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; OrderedLocusNames=DR_2111;
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: 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_CP015081.1.
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 EnsemblBacteria; AAF11660; AAF11660; DR_2111.
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 OMA; KPDPYKG; -.
DR OrthoDB; 1398618at2; -.
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; -; 2.
DR HAMAP; MF_01365_B; Ribosomal_L6_B; 1.
DR InterPro; IPR000702; Ribosomal_L6.
DR InterPro; IPR020040; Ribosomal_L6_a/b-dom.
DR InterPro; IPR036789; Ribosomal_L6_a/b-dom_sf.
DR InterPro; IPR019906; Ribosomal_L6_bac-type.
DR PANTHER; PTHR11655; PTHR11655; 1.
DR PANTHER; PTHR11655:SF14; PTHR11655:SF14; 1.
DR Pfam; PF00347; Ribosomal_L6; 2.
DR PIRSF; PIRSF002162; Ribosomal_L6; 1.
DR PRINTS; PR00059; RIBOSOMALL6.
DR SUPFAM; SSF56053; SSF56053; 2.
DR TIGRFAMs; TIGR03654; L6_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 CHAIN 1..185
FT /note="50S ribosomal protein L6"
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
