ID   RL11_ECO81              Reviewed;         142 AA.
AC   B7MRA9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN   Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=ECED1_4690;
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928162; CAR10797.2; -; Genomic_DNA.
DR   RefSeq; WP_001085926.1; NC_011745.1.
DR   AlphaFoldDB; B7MRA9; -.
DR   SMR; B7MRA9; -.
DR   EnsemblBacteria; CAR10797; CAR10797; ECED1_4690.
DR   GeneID; 67415316; -.
DR   KEGG; ecq:ECED1_4690; -.
DR   HOGENOM; CLU_074237_2_0_6; -.
DR   OMA; CKQFNAK; -.
DR   Proteomes; UP000000748; 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; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..142
FT                   /note="50S ribosomal protein L11"
FT                   /id="PRO_1000195637"
SQ   SEQUENCE   142 AA;  14875 MW;  C49226BB2462BE0F CRC64;
     MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNAKTDSIE KGLPIPVVIT
     VYADRSFTFV TKTPPAAVLL KKAAGIKSGS GKPNKDKVGK ISRAQLQEIA QTKAADMTGA
     DIEAMTRSIE GTARSMGLVV ED