(data stored in ACNUC7421 zone)

SWISSPROT: RL11_BACSU

ID   RL11_BACSU              Reviewed;         141 AA.
AC   Q06796;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   11-DEC-2019, entry version 125.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
DE            Short=BL11;
GN   Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; Synonyms=relC, tsp6;
GN   OrderedLocusNames=BSU01020;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ANTIBIOTIC RESISTANCE.
RX   PubMed=7968510; DOI=10.1111/j.1365-2958.1993.tb00910.x;
RA   Jeong S., Yoshikawa H., Takahashi H.;
RT   "Isolation and characterization of the secE homologue gene of Bacillus
RT   subtilis.";
RL   Mol. Microbiol. 10:133-142(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 35.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
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 2 L12 dimers bind in a sequential
CC       fashion forming a pentameric L10(L12)2(L12)2 complex.
CC   -!- PTM: One or more lysine residues are methylated. {ECO:0000255|HAMAP-
CC       Rule:MF_00736}.
CC   -!- MISCELLANEOUS: An unidentified mutation in this gene gives rise to
CC       thiostrepton resistance.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00736}.
DR   EMBL; D13303; BAA02561.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11878.2; -; Genomic_DNA.
DR   PIR; S39860; S39860.
DR   RefSeq; NP_387983.2; NC_000964.3.
DR   RefSeq; WP_003156430.1; NZ_JNCM01000029.1.
DR   PDB; 3J3V; EM; 13.30 A; 6=1-141.
DR   PDB; 3J3W; EM; 10.70 A; 6=1-141.
DR   PDB; 3J9W; EM; 3.90 A; BK=1-141.
DR   PDBsum; 3J3V; -.
DR   PDBsum; 3J3W; -.
DR   PDBsum; 3J9W; -.
DR   SMR; Q06796; -.
DR   STRING; 224308.BSU01020; -.
DR   jPOST; Q06796; -.
DR   PaxDb; Q06796; -.
DR   PRIDE; Q06796; -.
DR   EnsemblBacteria; CAB11878; CAB11878; BSU01020.
DR   GeneID; 33964332; -.
DR   GeneID; 936838; -.
DR   KEGG; bsu:BSU01020; -.
DR   PATRIC; fig|224308.179.peg.105; -.
DR   eggNOG; ENOG4108UIK; Bacteria.
DR   eggNOG; COG0080; LUCA.
DR   HOGENOM; HOG000082123; -.
DR   InParanoid; Q06796; -.
DR   KO; K02867; -.
DR   OMA; CKQFNAK; -.
DR   PhylomeDB; Q06796; -.
DR   BioCyc; BSUB:BSU01020-MONOMER; -.
DR   PRO; PR:Q06796; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
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   1: Evidence at protein level;
DR   PRODOM; Q06796.
DR   SWISS-2DPAGE; Q06796.
KW   3D-structure; Antibiotic resistance; Methylation; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..141
FT                   /note="50S ribosomal protein L11"
FT                   /id="PRO_0000104245"
FT   CONFLICT        35
FT                   /note="I -> V (in Ref. 1; BAA02561)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   141 AA;  14931 MW;  B2DA2178FD15E514 CRC64;
     MAKKVVKVVK LQIPAGKANP APPVGPALGQ AGVNIMGFCK EFNARTADQA GLIIPVEISV
     YEDRSFTFIT KTPPAAVLLK KAAGIESGSG EPNRNKVATV KRDKVREIAE TKMPDLNAAD
     VEAAMRMVEG TARSMGIVIE D
//

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