(data stored in ACNUC7421 zone)

SWISSPROT: D6XV92_BACIE

ID   D6XV92_BACIE            Unreviewed;       155 AA.
AC   D6XV92;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000256|HAMAP-Rule:MF_00736, ECO:0000256|SAAS:SAAS00731162};
GN   Name=rplK {ECO:0000256|HAMAP-Rule:MF_00736};
GN   OrderedLocusNames=Bsel_0101 {ECO:0000313|EMBL:ADH97650.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97650.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97650.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms part of the ribosomal stalk which helps the
CC       ribosome interact with GTP-bound translation factors.
CC       {ECO:0000256|HAMAP-Rule:MF_00736, ECO:0000256|RuleBase:RU003979,
CC       ECO:0000256|SAAS:SAAS00731150}.
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:0000256|HAMAP-Rule:MF_00736, ECO:0000256|SAAS:SAAS00731135}.
CC   -!- PTM: One or more lysine residues are methylated.
CC       {ECO:0000256|HAMAP-Rule:MF_00736, ECO:0000256|RuleBase:RU003979}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL11
CC       family. {ECO:0000256|HAMAP-Rule:MF_00736,
CC       ECO:0000256|RuleBase:RU003979, ECO:0000256|SAAS:SAAS01082579}.
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DR   EMBL; CP001791; ADH97650.1; -; Genomic_DNA.
DR   STRING; 439292.Bsel_0101; -.
DR   EnsemblBacteria; ADH97650; ADH97650; Bsel_0101.
DR   KEGG; bse:Bsel_0101; -.
DR   eggNOG; ENOG4108UIK; Bacteria.
DR   eggNOG; COG0080; LUCA.
DR   HOGENOM; HOG000082123; -.
DR   KO; K02867; -.
DR   OMA; CKQFNAK; -.
DR   BioCyc; BSEL439292:G1GLR-125-MONOMER; -.
DR   Proteomes; UP000000271; 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;
DR   PRODOM; D6XV92.
DR   SWISS-2DPAGE; D6XV92.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Methylation {ECO:0000256|HAMAP-Rule:MF_00736,
KW   ECO:0000256|RuleBase:RU003979};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_00736,
KW   ECO:0000256|RuleBase:RU003978, ECO:0000256|SAAS:SAAS00021678};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_00736,
KW   ECO:0000256|RuleBase:RU003978, ECO:0000256|SAAS:SAAS00426274,
KW   ECO:0000313|EMBL:ADH97650.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00736,
KW   ECO:0000256|RuleBase:RU003979, ECO:0000256|SAAS:SAAS00731127};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00736,
KW   ECO:0000256|RuleBase:RU003979, ECO:0000256|SAAS:SAAS00731155}.
FT   DOMAIN       16     80       Ribosomal_L11_N. {ECO:0000259|Pfam:
FT                                PF03946}.
FT   DOMAIN       85    153       Ribosomal_L11. {ECO:0000259|Pfam:
FT                                PF00298}.
SQ   SEQUENCE   155 AA;  16471 MW;  D3141FFF3E97D0AC CRC64;
     MLGLPHHGLK EVCRVAKKVI KVVKLQIPAG KANPAPPVGP ALGQAGVNIM GFCKEFNART
     QEDAGLIIPV EITVFEDRSF TFITKTPPAA VLLKKAAGID SGSGEPNKNK VATIKRDKVK
     EIAETKMPDL NAADVEAAMR MVEGTARSMG IVVED
//

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