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RL11_LIBAS
ID   RL11_LIBAS              Reviewed;         142 AA.
AC   P36250;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN   Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736};
OS   Liberibacter asiaticus (Citrus greening disease) (Liberobacter asiaticum).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=34021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7763375; DOI=10.1007/bf01577372;
RA   Villechanoux S., Garnier M., Laigret F., Renaudin J., Bove J.M.;
RT   "The genome of the non-cultured, bacterial-like organism associated with
RT   citrus greening disease contains the nusG-rplKAJL-rpoBC gene cluster and
RT   the gene for a bacteriophage type DNA polymerase.";
RL   Curr. Microbiol. 26:161-166(1993).
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; M94319; AAA23105.1; -; Genomic_DNA.
DR   RefSeq; WP_012778367.1; NZ_WOXD01000001.1.
DR   AlphaFoldDB; P36250; -.
DR   SMR; P36250; -.
DR   GeneID; 66285621; -.
DR   OMA; CKQFNAK; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..142
FT                   /note="50S ribosomal protein L11"
FT                   /id="PRO_0000104308"
SQ   SEQUENCE   142 AA;  15017 MW;  0EFD998ACA0226E7 CRC64;
     MAKVVSRIVK LQIESGSAKP SPPVGPAIGQ AGIPIMAFCK AFNAATEGME KGIPIPTTVT
     CYKDKSFTFT MSQPPVSFFL KKEVGIKSGS KLPGKESCGS ITRENIRKIA QLKMQDMGAI
     DIEGAMRMVE GSACSMGISV VD
 
 
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