ID   RL11_HAEDU              Reviewed;         142 AA.
AC   O32613;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN   Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=HD_1884;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-142.
RC   STRAIN=ATCC 33922 / 35000;
RA   Waring A.L., Parsons L.M.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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; AE017143; AAP96613.1; -; Genomic_DNA.
DR   EMBL; AF009342; AAB63583.1; -; Genomic_DNA.
DR   RefSeq; WP_005599211.1; NC_002940.2.
DR   AlphaFoldDB; O32613; -.
DR   SMR; O32613; -.
DR   STRING; 233412.HD_1884; -.
DR   EnsemblBacteria; AAP96613; AAP96613; HD_1884.
DR   GeneID; 60733464; -.
DR   GeneID; 66258475; -.
DR   KEGG; hdu:HD_1884; -.
DR   eggNOG; COG0080; Bacteria.
DR   HOGENOM; CLU_074237_2_0_6; -.
DR   OMA; CKQFNAK; -.
DR   Proteomes; UP000001022; 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; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..142
FT                   /note="50S ribosomal protein L11"
FT                   /id="PRO_0000104293"
FT   CONFLICT        83
FT                   /note="A -> R (in Ref. 2; AAB63583)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   142 AA;  14962 MW;  1C43805D8FCB0BFB CRC64;
     MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNARTESLE KGLPIPVVIT
     VYADRSFTFV TKTPPAAVLL KKAVGIKSGS GKPNKDKVGT VTQEQLRQIA ETKAADMTGA
     TIETKMKSIA GTARSMGLIV EE