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 03-AUG-2022, entry version 135.
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}.
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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 PDB; 7AQC; EM; 2.99 A; I=1-141.
DR PDB; 7AQD; EM; 3.10 A; I=1-141.
DR PDB; 7AS8; EM; 2.90 A; K=1-141.
DR PDB; 7AS9; EM; 3.50 A; K=1-141.
DR PDB; 7ASA; EM; 3.50 A; K=1-141.
DR PDB; 7O5B; EM; 3.33 A; q=1-141.
DR PDB; 7OPE; EM; 3.20 A; K=1-141.
DR PDBsum; 3J3V; -.
DR PDBsum; 3J3W; -.
DR PDBsum; 3J9W; -.
DR PDBsum; 7AQC; -.
DR PDBsum; 7AQD; -.
DR PDBsum; 7AS8; -.
DR PDBsum; 7AS9; -.
DR PDBsum; 7ASA; -.
DR PDBsum; 7O5B; -.
DR PDBsum; 7OPE; -.
DR AlphaFoldDB; Q06796; -.
DR SMR; Q06796; -.
DR IntAct; Q06796; 21.
DR STRING; 224308.BSU01020; -.
DR jPOST; Q06796; -.
DR PaxDb; Q06796; -.
DR PRIDE; Q06796; -.
DR EnsemblBacteria; CAB11878; CAB11878; BSU_01020.
DR GeneID; 64301940; -.
DR GeneID; 66327877; -.
DR GeneID; 936838; -.
DR KEGG; bsu:BSU01020; -.
DR PATRIC; fig|224308.179.peg.105; -.
DR eggNOG; COG0080; Bacteria.
DR InParanoid; Q06796; -.
DR OMA; CKQFNAK; -.
DR PhylomeDB; Q06796; -.
DR BioCyc; BSUB:BSU01020-MON; -.
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:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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;
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"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:7AQC"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7AS9"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:7AS8"
SQ SEQUENCE 141 AA; 14931 MW; B2DA2178FD15E514 CRC64;
MAKKVVKVVK LQIPAGKANP APPVGPALGQ AGVNIMGFCK EFNARTADQA GLIIPVEISV
YEDRSFTFIT KTPPAAVLLK KAAGIESGSG EPNRNKVATV KRDKVREIAE TKMPDLNAAD
VEAAMRMVEG TARSMGIVIE D
