ID   RL11_PHYMT              Reviewed;         141 AA.
AC   B3QZG6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN   Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=ATP_00386;
OS   Phytoplasma mali (strain AT).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; 16SrX (Apple proliferation group).
OX   NCBI_TaxID=482235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT;
RX   PubMed=18582369; DOI=10.1186/1471-2164-9-306;
RA   Kube M., Schneider B., Kuhl H., Dandekar T., Heitmann K., Migdoll A.M.,
RA   Reinhardt R., Seemueller E.;
RT   "The linear chromosome of the plant-pathogenic mycoplasma 'Candidatus
RT   Phytoplasma mali'.";
RL   BMC Genomics 9:306-306(2008).
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; CU469464; CAP18573.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3QZG6; -.
DR   SMR; B3QZG6; -.
DR   STRING; 37692.ATP_00386; -.
DR   EnsemblBacteria; CAP18573; CAP18573; ATP_00386.
DR   KEGG; pml:ATP_00386; -.
DR   eggNOG; COG0080; Bacteria.
DR   HOGENOM; CLU_074237_2_0_14; -.
DR   OMA; CKQFNAK; -.
DR   Proteomes; UP000002020; 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   3: Inferred from homology;
KW   Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..141
FT                   /note="50S ribosomal protein L11"
FT                   /id="PRO_1000195688"
SQ   SEQUENCE   141 AA;  15192 MW;  AA85260E361F2D29 CRC64;
     MAKQVVKKIK LQILAGKANP APPVGPALGQ AQVNIPSFCS QFNEATKDQA NYLVTAVISV
     YNDRSFTFII KTPPASSLLK KAANIKLGSA NSNKNKVATI KFDQIKEIAT LKMPDLNAYT
     LESACKIIEG TARNMGIIVE K