RL11_VIBVY
ID RL11_VIBVY Reviewed; 142 AA.
AC P60105; Q7MGR4;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=VV3163;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC95927.1; -; Genomic_DNA.
DR RefSeq; WP_011151383.1; NC_005139.1.
DR AlphaFoldDB; P60105; -.
DR SMR; P60105; -.
DR STRING; 672.VV93_v1c28800; -.
DR EnsemblBacteria; BAC95927; BAC95927; BAC95927.
DR GeneID; 59229929; -.
DR KEGG; vvy:VV3163; -.
DR PATRIC; fig|196600.6.peg.3132; -.
DR eggNOG; COG0080; Bacteria.
DR HOGENOM; CLU_074237_2_0_6; -.
DR OMA; CKQFNAK; -.
DR OrthoDB; 1702697at2; -.
DR Proteomes; UP000002675; Chromosome I.
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..142
FT /note="50S ribosomal protein L11"
FT /id="PRO_0000104410"
SQ SEQUENCE 142 AA; 14781 MW; 346258663A58D9AC CRC64;
MAKKVEAYIK LQVAAGMANP SPPVGPALGQ RGVNIMEFCK AFNAKTESME KGLPVPVVIT
VYSDRSFTFV TKTPPAAVLL KKAAGIKSGS GRPNTEKVGT VTDAQIQEIA EAKAADMTGA
DIEAMKRSIA GTARSMGLVV EG