ID   RL11_THICR              Reviewed;         142 AA.
AC   Q31IZ3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   01-MAY-2013, entry version 54.
DE   RecName: Full=50S ribosomal protein L11;
GN   Name=rplK; OrderedLocusNames=Tcr_0284;
OS   Thiomicrospira crunogena (strain XCL-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=317025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XCL-2;
RX   PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA   Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J.,
RA   Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R.,
RA   Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A.,
RA   Freyermuth S.K., Harmer T.L., Hauser L.J., Huegler M., Kerfeld C.A.,
RA   Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L.,
RA   Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z.,
RA   Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T.,
RA   Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E.,
RA   Zeruth G.T.;
RT   "The genome of deep-sea vent chemolithoautotroph Thiomicrospira
RT   crunogena XCL-2.";
RL   PLoS Biol. 4:1-17(2006).
CC   -!- FUNCTION: This protein binds directly to 23S ribosomal RNA (By
CC       similarity).
CC   -!- PTM: One or more lysine residues are methylated (By similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L11P family.
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DR   EMBL; CP000109; ABB40880.1; -; Genomic_DNA.
DR   RefSeq; YP_390554.1; NC_007520.2.
DR   HSSP; Q5SLP6; 1YL3.
DR   ProteinModelPortal; Q31IZ3; -.
DR   SMR; Q31IZ3; 2-141.
DR   STRING; 317025.Tcr_0284; -.
DR   EnsemblBacteria; ABB40880; ABB40880; Tcr_0284.
DR   GeneID; 3760666; -.
DR   KEGG; tcx:Tcr_0284; -.
DR   PATRIC; 23972454; VBIThiCru83387_0295.
DR   eggNOG; COG0080; -.
DR   HOGENOM; HOG000082123; -.
DR   KO; K02867; -.
DR   OMA; KQFNAKT; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:HAMAP.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:HAMAP.
DR   Gene3D; 1.10.10.250; -; 1.
DR   Gene3D; 3.30.1550.10; -; 1.
DR   HAMAP; MF_00736_B; Ribosomal_L11_B; 1; -.
DR   InterPro; IPR000911; Ribosomal_L11.
DR   InterPro; IPR006519; Ribosomal_L11_bac-typ.
DR   InterPro; IPR020783; Ribosomal_L11_C.
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; Ribosomal_L11; 1.
DR   SUPFAM; SSF54747; Ribosomal_L11; 1.
DR   TIGRFAMs; TIGR01632; L11_bact; 1.
DR   PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Methylation; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN         1    142       50S ribosomal protein L11.
FT                                /FTId=PRO_0000258236.
SQ   SEQUENCE   142 AA;  14947 MW;  0ABD2F6A5B020ED5 CRC64;
     MAKKIEAYIK LQVPAGNANP SPPVGPALGQ HGVNIMEFCK AFNAQTQSME KNLPVPVVIT
     VFNDRSFTFI TKTPPASVLL KKAAGIQKGS GVPNMDKVGT VTRAQLEEIA NTKMADLNAN
     DLDAAVKIIA GSARSMGLNV EG
//