ID   RL11_STRVG              Reviewed;         144 AA.
AC   P27310;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN   Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736};
OS   Streptomyces virginiae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces virginiae group.
OX   NCBI_TaxID=1961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MAFF10-06014;
RX   PubMed=1309760; DOI=10.1016/s0021-9258(18)48400-1;
RA   Okamoto S., Nihirra T., Kataoka H., Suzuki A., Yamada Y.;
RT   "Purification and molecular cloning of a butyrolactone autoregulator
RT   receptor from Streptomyces virginiae.";
RL   J. Biol. Chem. 267:1093-1098(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8675024; DOI=10.1016/0378-1119(96)00067-4;
RA   Katayama M., Sakai Y., Okamoto S., Ihara F., Nihira T., Yamada Y.;
RT   "Gene organization in the ada-rplL region of Streptomyces virginiae.";
RL   Gene 171:135-136(1996).
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; D10469; BAA01263.1; -; Genomic_DNA.
DR   EMBL; D10468; BAA01262.1; -; Genomic_DNA.
DR   EMBL; D50624; BAA09302.1; -; Genomic_DNA.
DR   PIR; B41773; B41773.
DR   RefSeq; WP_030008445.1; NZ_LGUV01000155.1.
DR   AlphaFoldDB; P27310; -.
DR   SMR; P27310; -.
DR   STRING; 1961.JOAK01000021_gene7138; -.
DR   eggNOG; COG0080; Bacteria.
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   3: Inferred from homology;
KW   Methylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..144
FT                   /note="50S ribosomal protein L11"
FT                   /id="PRO_0000104390"
SQ   SEQUENCE   144 AA;  15197 MW;  8FA61EABAA6070B8 CRC64;
     MPPKKKKVTG LIKLQIKAGA ANPAPPVGPA LGQHGVNIME FCKAYNAATE SQRGMVVPVE
     ITVYDDRSFT FITKTPPAAR LILKHAGIEK GSGEPHKTKV AKLTAAQVKE IAELKMPDLN
     ANDIDAAVKI IAGTARSMGV TVEG