(data stored in ACNUC29543 zone)

SWISSPROT: RL11_ACIBT

ID   RL11_ACIBT              Reviewed;         142 AA.
AC   A3M1F9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAY-2019, 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=A1S_0283;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
CC   -!- FUNCTION: Forms part of the ribosomal stalk which helps the
CC       ribosome interact with GTP-bound translation factors.
CC       {ECO:0000255|HAMAP-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
CC       stalk. L10 forms an elongated spine to which L12 dimers bind in a
CC       sequential fashion forming a multimeric L10(L12)X complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00736}.
CC   -!- PTM: One or more lysine residues are methylated.
CC       {ECO:0000255|HAMAP-Rule:MF_00736}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL11
CC       family. {ECO:0000255|HAMAP-Rule:MF_00736}.
DR   EMBL; CP000521; ABO10753.2; -; Genomic_DNA.
DR   SMR; A3M1F9; -.
DR   EnsemblBacteria; ABO10753; ABO10753; A1S_0283.
DR   KEGG; acb:A1S_0283; -.
DR   HOGENOM; HOG000082123; -.
DR   KO; K02867; -.
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;
DR   PRODOM; A3M1F9.
DR   SWISS-2DPAGE; A3M1F9.
KW   Methylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN         1    142       50S ribosomal protein L11.
FT                                /FTId=PRO_1000132850.
SQ   SEQUENCE   142 AA;  15044 MW;  A207E76B611C86E6 CRC64;
     MAKKIDGYIK LQVPAGKANP SPPIGPALGQ RGVNIMAFCK EFNAATQKVE PGLPIPVVIT
     VYNDKSFTFI MKTPPASILL KKAAGIQKGS SVPNKTKVGK LTRAQLEEIA TTKEPDLTGA
     DLDARVRTIA GSARSMGLEV EL
//

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