RL11_THET2
ID RL11_THET2 Reviewed; 147 AA.
AC P62442;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=TT_C1738;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
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; AE017221; AAS82080.1; -; Genomic_DNA.
DR RefSeq; WP_011174097.1; NC_005835.1.
DR PDB; 4V9J; X-ray; 3.86 A; BK/DK=2-141.
DR PDB; 4V9K; X-ray; 3.50 A; BK/DK=2-141.
DR PDB; 4V9L; X-ray; 3.50 A; BK/DK=2-141.
DR PDB; 4V9M; X-ray; 4.00 A; BK/DK=2-141.
DR PDB; 4V9N; X-ray; 3.40 A; BK/DK=1-147.
DR PDB; 4W29; X-ray; 3.80 A; BK/DK=2-141.
DR PDB; 4XEJ; X-ray; 3.80 A; AL11/BL11=1-147.
DR PDBsum; 4V9J; -.
DR PDBsum; 4V9K; -.
DR PDBsum; 4V9L; -.
DR PDBsum; 4V9M; -.
DR PDBsum; 4V9N; -.
DR PDBsum; 4W29; -.
DR PDBsum; 4XEJ; -.
DR AlphaFoldDB; P62442; -.
DR BMRB; P62442; -.
DR SMR; P62442; -.
DR IntAct; P62442; 2.
DR STRING; 262724.TT_C1738; -.
DR EnsemblBacteria; AAS82080; AAS82080; TT_C1738.
DR GeneID; 3168343; -.
DR KEGG; tth:TT_C1738; -.
DR eggNOG; COG0080; Bacteria.
DR HOGENOM; CLU_074237_2_0_0; -.
DR OMA; CKQFNAK; -.
DR OrthoDB; 1702697at2; -.
DR Proteomes; UP000000592; 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; Methylation; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..147
FT /note="50S ribosomal protein L11"
FT /id="PRO_0000104398"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:4V9L"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4V9N"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:4V9N"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:4V9N"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4V9N"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:4V9N"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4V9N"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4V9N"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:4V9N"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:4V9N"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:4V9L"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:4V9N"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:4V9N"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:4V9N"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4V9L"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:4V9N"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:4V9N"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4V9N"
SQ SEQUENCE 147 AA; 15505 MW; 3D8DECEBE85B5FE9 CRC64;
MKKVVAVVKL QLPAGKATPA PPVGPALGQH GANIMEFVKA FNAATANMGD AIVPVEITIY
ADRSFTFVTK TPPASYLIRK AAGLEKGAHK PGREKVGRIT WEQVLEIAKQ KMPDLNTTDL
EAAARMIAGS ARSMGVEVVG APEVKDA
