RL11_THET8
ID RL11_THET8 Reviewed; 147 AA.
AC Q5SLP6;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=TTHA0247;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=1447157; DOI=10.1128/jb.174.23.7859-7863.1992;
RA Heinrich T., Schroeder W., Erdmann V.A., Hartmann R.K.;
RT "Identification of the gene encoding transcription factor NusG of Thermus
RT thermophilus.";
RL J. Bacteriol. 174:7859-7863(1992).
RN [3]
RP PROTEIN SEQUENCE OF 19-32 AND 71-85, AND BLOCKAGE OF N-TERMINUS.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=11154066; DOI=10.1515/bc.2000.133;
RA Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H.,
RA Choli-Papadopoulou T.;
RT "Identification of the 50S ribosomal proteins from the eubacterium Thermus
RT thermophilus.";
RL Biol. Chem. 381:1079-1087(2000).
RN [4]
RP METHYLATION AT LYS-3.
RX PubMed=10333296; DOI=10.1023/a:1020684224200;
RA Triantafillidou D., Simitsopoulou M., Franceschi F., Choli-Papadopoulou T.;
RT "Structural and functional studies on the overproduced L11 protein from
RT Thermus thermophilus.";
RL J. Protein Chem. 18:215-223(1999).
RN [5]
RP MASS SPECTROMETRY, AND METHYLATION.
RX PubMed=15317787; DOI=10.1128/jb.186.17.5819-5825.2004;
RA Cameron D.M., Gregory S.T., Thompson J., Suh M.-J., Limbach P.A.,
RA Dahlberg A.E.;
RT "Thermus thermophilus L11 methyltransferase, PrmA, is dispensable for
RT growth and preferentially modifies free ribosomal protein L11 prior to
RT ribosome assembly.";
RL J. Bacteriol. 186:5819-5825(2004).
RN [6]
RP MASS SPECTROMETRY.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=16287167; DOI=10.1002/pmic.200402111;
RA Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.;
RT "Extending ribosomal protein identifications to unsequenced bacterial
RT strains using matrix-assisted laser desorption/ionization mass
RT spectrometry.";
RL Proteomics 5:4818-4831(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
RX PubMed=11511350; DOI=10.1016/s0092-8674(01)00435-4;
RA Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.;
RT "The path of messenger RNA through the ribosome.";
RL Cell 106:233-241(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
RX PubMed=11283358; DOI=10.1126/science.1060089;
RA Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N.,
RA Cate J.H.D., Noller H.F.;
RT "Crystal structure of the ribosome at 5.5 A resolution.";
RL Science 292:883-896(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (6.46 ANGSTROMS) OF 70S RIBOSOME, AND SUBUNIT.
RX PubMed=16377566; DOI=10.1016/j.cell.2005.09.039;
RA Petry S., Brodersen D.E., Murphy F.V., Dunham C.M., Selmer M., Tarry M.J.,
RA Kelley A.C., Ramakrishnan V.;
RT "Crystal structures of the ribosome in complex with release factors RF1 and
RT RF2 bound to a cognate stop codon.";
RL Cell 123:1255-1266(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-147, AND METHYLATION AT MET-1
RP AND LYS-39.
RX PubMed=18611379; DOI=10.1016/j.str.2008.03.016;
RA Demirci H., Gregory S.T., Dahlberg A.E., Jogl G.;
RT "Multiple-site trimethylation of ribosomal protein L11 by the PrmA
RT methyltransferase.";
RL Structure 16:1059-1066(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH RF2,
RP INTERACTION WITH RF2, AND SUBUNIT.
RX PubMed=18988853; DOI=10.1126/science.1164840;
RA Weixlbaumer A., Jin H., Neubauer C., Voorhees R.M., Petry S., Kelley A.C.,
RA Ramakrishnan V.;
RT "Insights into translational termination from the structure of RF2 bound to
RT the ribosome.";
RL Science 322:953-956(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH RF2,
RP AND SUBUNIT.
RX PubMed=20421507; DOI=10.1073/pnas.1003995107;
RA Jin H., Kelley A.C., Loakes D., Ramakrishnan V.;
RT "Structure of the 70S ribosome bound to release factor 2 and a substrate
RT analog provides insights into catalysis of peptide release.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8593-8598(2010).
CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors. The stalk extends beyond
CC the surface of the 70S ribosome and is preferentially stabilized in 70S
CC versus 50S crystals.
CC -!- FUNCTION: In the 70S ribosome is in a position where it could interact
CC transiently with the A site tRNA during translation.
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 3 L12 dimers bind in a sequential
CC fashion forming a heptameric L10(L12)2(L12)2(L12)2 complex. Contacts
CC one of the L7 dimers. Interacts with RF2 (release factor 2)
CC (PubMed:18988853). {ECO:0000269|PubMed:11283358,
CC ECO:0000269|PubMed:11511350, ECO:0000269|PubMed:18988853}.
CC -!- PTM: The protein probably contains twelve methyl groups; at least one
CC lysine residue (Lys-3) is known to be trimethylated. Methylation of the
CC protein is not required for function. {ECO:0000269|PubMed:10333296,
CC ECO:0000269|PubMed:15317787}.
CC -!- MASS SPECTROMETRY: Mass=15506.2; Method=MALDI; Note=Weight of the
CC unmethylated protein.; Evidence={ECO:0000269|PubMed:15317787};
CC -!- MASS SPECTROMETRY: Mass=15675.1; Method=MALDI; Note=Weight of the
CC methylated protein.; Evidence={ECO:0000269|PubMed:15317787};
CC -!- MASS SPECTROMETRY: Mass=15678; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16287167};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000255|HAMAP-Rule:MF_00736}.
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DR EMBL; AP008226; BAD70070.1; -; Genomic_DNA.
DR EMBL; L10348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_011174097.1; NC_006461.1.
DR RefSeq; YP_143513.1; NC_006461.1.
DR PDB; 3EGV; X-ray; 1.75 A; B=2-147.
DR PDB; 4V42; X-ray; 5.50 A; BL=9-116.
DR PDB; 4V4P; X-ray; 5.50 A; L=6-116.
DR PDB; 4V4T; X-ray; 6.46 A; K=1-141.
DR PDB; 4V4X; X-ray; 5.00 A; BL=1-147.
DR PDB; 4V4Y; X-ray; 5.50 A; BL=1-147.
DR PDB; 4V4Z; X-ray; 4.51 A; BL=1-147.
DR PDB; 4V51; X-ray; 2.80 A; K=1-147.
DR PDB; 4V5E; X-ray; 3.45 A; BK/DK=1-147.
DR PDB; 4V5F; X-ray; 3.60 A; BK/DK=1-147.
DR PDB; 4V5J; X-ray; 3.10 A; BK/DK=1-147.
DR PDB; 4V5M; EM; 7.80 A; BK=1-147.
DR PDB; 4V5N; EM; 7.60 A; BK=1-147.
DR PDB; 4V68; EM; 6.40 A; BL=2-139.
DR PDB; 4V6F; X-ray; 3.10 A; DL=1-147.
DR PDB; 4V9H; X-ray; 2.86 A; BK=1-147.
DR PDB; 4W2E; X-ray; 2.90 A; K=1-147.
DR PDB; 4WPO; X-ray; 2.80 A; AL/CL=1-147.
DR PDB; 4WQF; X-ray; 2.80 A; AL/CL=1-147.
DR PDB; 4WQU; X-ray; 2.80 A; AL/CL=1-147.
DR PDB; 4WQY; X-ray; 2.80 A; AL/CL=1-147.
DR PDB; 5A9Z; EM; 4.70 A; AJ=4-137.
DR PDB; 5AA0; EM; 5.00 A; AJ=4-137.
DR PDB; 5D8B; X-ray; 3.63 A; CB/G=1-147.
DR PDB; 5HAU; X-ray; 3.00 A; 1K/2K=1-147.
DR PDB; 5IMQ; EM; 3.80 A; 3=1-147.
DR PDB; 5IMR; EM; -; 3=1-147.
DR PDB; 5J8B; X-ray; 2.60 A; K=1-147.
DR PDB; 5ZLU; EM; 3.60 A; f=1-147.
DR PDB; 6C5L; X-ray; 3.20 A; BK/DK=1-147.
DR PDB; 6GSL; X-ray; 3.16 A; 48=1-147.
DR PDBsum; 3EGV; -.
DR PDBsum; 4V42; -.
DR PDBsum; 4V4P; -.
DR PDBsum; 4V4T; -.
DR PDBsum; 4V4X; -.
DR PDBsum; 4V4Y; -.
DR PDBsum; 4V4Z; -.
DR PDBsum; 4V51; -.
DR PDBsum; 4V5E; -.
DR PDBsum; 4V5F; -.
DR PDBsum; 4V5J; -.
DR PDBsum; 4V5M; -.
DR PDBsum; 4V5N; -.
DR PDBsum; 4V68; -.
DR PDBsum; 4V6F; -.
DR PDBsum; 4V9H; -.
DR PDBsum; 4W2E; -.
DR PDBsum; 4WPO; -.
DR PDBsum; 4WQF; -.
DR PDBsum; 4WQU; -.
DR PDBsum; 4WQY; -.
DR PDBsum; 5A9Z; -.
DR PDBsum; 5AA0; -.
DR PDBsum; 5D8B; -.
DR PDBsum; 5HAU; -.
DR PDBsum; 5IMQ; -.
DR PDBsum; 5IMR; -.
DR PDBsum; 5J8B; -.
DR PDBsum; 5ZLU; -.
DR PDBsum; 6C5L; -.
DR PDBsum; 6GSL; -.
DR AlphaFoldDB; Q5SLP6; -.
DR BMRB; Q5SLP6; -.
DR SMR; Q5SLP6; -.
DR IntAct; Q5SLP6; 47.
DR MINT; Q5SLP6; -.
DR STRING; 300852.55771629; -.
DR EnsemblBacteria; BAD70070; BAD70070; BAD70070.
DR GeneID; 3168343; -.
DR KEGG; ttj:TTHA0247; -.
DR PATRIC; fig|300852.9.peg.247; -.
DR eggNOG; COG0080; Bacteria.
DR HOGENOM; CLU_074237_2_0_0; -.
DR OMA; CKQFNAK; -.
DR PhylomeDB; Q5SLP6; -.
DR EvolutionaryTrace; Q5SLP6; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
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..147
FT /note="50S ribosomal protein L11"
FT /id="PRO_0000104399"
FT MOD_RES 1
FT /note="N,N,N-trimethylmethionine"
FT /evidence="ECO:0000269|PubMed:18611379,
FT ECO:0007744|PDB:3EGV"
FT MOD_RES 3
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:10333296"
FT MOD_RES 39
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:18611379,
FT ECO:0007744|PDB:3EGV"
FT MOD_RES 70
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0A7J7"
FT CONFLICT 20
FT /note="A -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="V -> G (in Ref. 2; L10348)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:3EGV"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:3EGV"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:3EGV"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:3EGV"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3EGV"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:3EGV"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3EGV"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:3EGV"
SQ SEQUENCE 147 AA; 15505 MW; 3D8DECEBE85B5FE9 CRC64;
MKKVVAVVKL QLPAGKATPA PPVGPALGQH GANIMEFVKA FNAATANMGD AIVPVEITIY
ADRSFTFVTK TPPASYLIRK AAGLEKGAHK PGREKVGRIT WEQVLEIAKQ KMPDLNTTDL
EAAARMIAGS ARSMGVEVVG APEVKDA
