RL11_DEIRA
ID RL11_DEIRA Reviewed; 144 AA.
AC Q9RSS7;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=DR_2046;
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: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors. {ECO:0000305}.
CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit.
CC Interacts with L10 and the large rRNA to form the base of the stalk.
CC L10 forms an elongated spine to which L12 dimers bind in a sequential
CC fashion forming a multimeric L10(L12)X complex (By similarity).
CC Contacts the CTC protein (RL25). {ECO:0000255|HAMAP-Rule:MF_00736,
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 -!- PTM: One or more lysine residues are methylated. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000255|HAMAP-Rule:MF_00736}.
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DR EMBL; AE000513; AAF11593.1; -; Genomic_DNA.
DR PIR; G75323; G75323.
DR RefSeq; NP_295769.1; NC_001263.1.
DR RefSeq; WP_010888678.1; NZ_CP015081.1.
DR PDB; 1NKW; X-ray; 3.10 A; G=1-144.
DR PDB; 1NWX; X-ray; 3.50 A; G=1-144.
DR PDB; 1NWY; X-ray; 3.30 A; G=1-144.
DR PDB; 1SM1; X-ray; 3.42 A; G=1-144.
DR PDB; 1XBP; X-ray; 3.50 A; G=1-144.
DR PDB; 2ZJP; X-ray; 3.70 A; F=1-144.
DR PDB; 2ZJQ; X-ray; 3.30 A; F=1-144.
DR PDB; 2ZJR; X-ray; 2.91 A; F=1-144.
DR PDB; 3CF5; X-ray; 3.30 A; F=1-144.
DR PDB; 3DLL; X-ray; 3.50 A; F=1-144.
DR PDB; 3PIO; X-ray; 3.25 A; F=1-144.
DR PDB; 3PIP; X-ray; 3.45 A; F=1-144.
DR PDB; 4IO9; X-ray; 3.20 A; F=1-144.
DR PDB; 4IOA; X-ray; 3.20 A; F=1-144.
DR PDB; 4IOC; X-ray; 3.60 A; F=1-144.
DR PDB; 4V49; X-ray; 8.70 A; G=1-143.
DR PDB; 4V4A; X-ray; 9.50 A; G=1-143.
DR PDB; 4V4G; X-ray; 11.50 A; J=1-143.
DR PDB; 5DM6; X-ray; 2.90 A; F=4-144.
DR PDB; 5DM7; X-ray; 3.00 A; F=1-144.
DR PDB; 5JVG; X-ray; 3.43 A; F=1-144.
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; 4V49; -.
DR PDBsum; 4V4A; -.
DR PDBsum; 4V4G; -.
DR PDBsum; 5DM6; -.
DR PDBsum; 5DM7; -.
DR PDBsum; 5JVG; -.
DR AlphaFoldDB; Q9RSS7; -.
DR SMR; Q9RSS7; -.
DR IntAct; Q9RSS7; 29.
DR STRING; 243230.DR_2046; -.
DR EnsemblBacteria; AAF11593; AAF11593; DR_2046.
DR KEGG; dra:DR_2046; -.
DR PATRIC; fig|243230.17.peg.2273; -.
DR eggNOG; COG0080; Bacteria.
DR HOGENOM; CLU_074237_2_1_0; -.
DR InParanoid; Q9RSS7; -.
DR OMA; CKQFNAK; -.
DR OrthoDB; 1702697at2; -.
DR EvolutionaryTrace; Q9RSS7; -.
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:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd00349; Ribosomal_L11; 1.
DR Gene3D; 1.10.10.250; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR InterPro; IPR006519; Ribosomal_L11_bac-typ.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR036769; Ribosomal_L11_C_sf.
DR InterPro; IPR020785; Ribosomal_L11_CS.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR TIGRFAMs; TIGR01632; L11_bact; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Methylation; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..144
FT /note="50S ribosomal protein L11"
FT /id="PRO_0000104280"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:5DM7"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:5DM7"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2ZJQ"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2ZJR"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 105..110
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2ZJQ"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 126..134
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2ZJR"
SQ SEQUENCE 144 AA; 14872 MW; F2DA3B99E230D207 CRC64;
MKKVAGIVKL QLPAGKATPA PPVGPALGQY GANIMEFTKA FNAQTADKGD AIIPVEITIY
ADRSFTFITK TPPMSYLIRK AAGIGKGSST PNKAKVGKLN WDQVLEIAKT KMPDLNAGSV
EAAANTVAGT ARSMGVTVEG GPNA
