ID   RL11_METJA              Reviewed;         161 AA.
AC   P54030;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN   Name=rpl11 {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=MJ0373;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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   -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00736}.
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DR   EMBL; L77117; AAB98362.1; -; Genomic_DNA.
DR   PIR; E64346; E64346.
DR   RefSeq; WP_010869872.1; NC_000909.1.
DR   PDB; 5COL; X-ray; 2.25 A; A/B=1-161.
DR   PDB; 5D8H; X-ray; 2.80 A; C=1-161.
DR   PDB; 5DAR; X-ray; 2.90 A; C/F=1-161.
DR   PDBsum; 5COL; -.
DR   PDBsum; 5D8H; -.
DR   PDBsum; 5DAR; -.
DR   AlphaFoldDB; P54030; -.
DR   SMR; P54030; -.
DR   STRING; 243232.MJ_0373; -.
DR   EnsemblBacteria; AAB98362; AAB98362; MJ_0373.
DR   GeneID; 1451230; -.
DR   KEGG; mja:MJ_0373; -.
DR   eggNOG; arCOG04372; Archaea.
DR   HOGENOM; CLU_074237_4_0_2; -.
DR   InParanoid; P54030; -.
DR   OMA; CKQFNAK; -.
DR   OrthoDB; 98187at2157; -.
DR   PhylomeDB; P54030; -.
DR   Proteomes; UP000000805; Chromosome.
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: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; 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   PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..161
FT                   /note="50S ribosomal protein L11"
FT                   /id="PRO_0000104435"
FT   STRAND          3..11
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:5D8H"
FT   HELIX           21..25
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   TURN            26..29
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   HELIX           32..42
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   HELIX           43..46
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   STRAND          49..58
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   STRAND          64..68
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   HELIX           73..81
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:5D8H"
FT   STRAND          96..98
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   HELIX           100..113
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   HELIX           119..132
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:5COL"
FT   HELIX           142..151
FT                   /evidence="ECO:0007829|PDB:5COL"
SQ   SEQUENCE   161 AA;  17490 MW;  2B3B00332D110A81 CRC64;
     MAKEVVEVLV TGGRATAGPP LGPAIGPLGV NVMQVVKEIN EKTKDYEGMQ VPVKVIVDTE
     TRKFEIEVGI PPTTALIKKE LGIETAAHEP RHEVVGNLTL EQVIKIAKMK KDAMLSYTLK
     NAVKEVLGTC GSMGVTVEGK DPKEVQKEID AGVYDEYFKE E