RL11_BACMK
ID RL11_BACMK Reviewed; 141 AA.
AC A9VNB0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736};
GN OrderedLocusNames=BcerKBAB4_0092;
OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000903; ABY41361.1; -; Genomic_DNA.
DR RefSeq; WP_001085872.1; NC_010184.1.
DR AlphaFoldDB; A9VNB0; -.
DR SMR; A9VNB0; -.
DR STRING; 315730.BcerKBAB4_0092; -.
DR EnsemblBacteria; ABY41361; ABY41361; BcerKBAB4_0092.
DR GeneID; 59159723; -.
DR GeneID; 64202506; -.
DR GeneID; 67504804; -.
DR KEGG; bwe:BcerKBAB4_0092; -.
DR eggNOG; COG0080; Bacteria.
DR HOGENOM; CLU_074237_2_1_9; -.
DR OMA; CKQFNAK; -.
DR Proteomes; UP000002154; 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..141
FT /note="50S ribosomal protein L11"
FT /id="PRO_1000132865"
SQ SEQUENCE 141 AA; 14976 MW; 8B683BB177F5D41D CRC64;
MAKKVIKMVK LQIPAGKANP APPVGPALGQ AGVNIMGFCK EFNARTADQA GLIIPVEITV
FEDRSFTFIT KTPPAAVLLK KVAGIESGSG EPNRNKVATV KRDKVREIAE TKMPDLNAAS
VEAAMRMVEG TARSMGIVIE D