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RL11_THEMA
ID   RL11_THEMA              Reviewed;         141 AA.
AC   P29395;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 163.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN   Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=TM_0454;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=1429627; DOI=10.1016/s0021-9258(18)50016-8;
RA   Liao D., Dennis P.P.;
RT   "The organization and expression of essential transcription translation
RT   component genes in the extremely thermophilic eubacterium Thermotoga
RT   maritima.";
RL   J. Biol. Chem. 267:22787-22797(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS).
RX   PubMed=10338213; DOI=10.1016/s0092-8674(00)80759-x;
RA   Wimberly B.T., Guymon R., McCutcheon J.P., White S.W., Ramakrishnan V.;
RT   "A detailed view of a ribosomal active site: the structure of the L11-RNA
RT   complex.";
RL   Cell 97:491-502(1999).
CC   -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC       interact with GTP-bound translation factors.
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 3 L12 dimers bind in a sequential
CC       fashion forming a heptameric L10(L12)2(L12)2(L12)2 complex.
CC   -!- PTM: One or more lysine residues are methylated. {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; Z11839; CAA77859.1; -; Genomic_DNA.
DR   EMBL; AE000512; AAD35537.1; -; Genomic_DNA.
DR   PIR; B44466; R5HG11.
DR   RefSeq; NP_228264.1; NC_000853.1.
DR   RefSeq; WP_004081512.1; NZ_CP011107.1.
DR   PDB; 1JQM; EM; -; A=2-140.
DR   PDB; 1JQS; EM; -; A=2-140.
DR   PDB; 1JQT; EM; -; A=2-140.
DR   PDB; 1ML5; EM; 14.00 A; l=1-141.
DR   PDB; 1MMS; X-ray; 2.57 A; A/B=2-141.
DR   PDB; 1MVR; EM; 12.80 A; L=2-141.
DR   PDB; 1OLN; NMR; -; A=2-141.
DR   PDB; 1PN7; EM; 10.80 A; L=8-140.
DR   PDB; 1PN8; EM; 10.80 A; L=8-140.
DR   PDB; 1R2W; EM; 9.00 A; A=2-141.
DR   PDB; 1R2X; EM; 9.00 A; A=2-141.
DR   PDB; 2BCW; EM; 11.20 A; A=8-72.
DR   PDB; 2JQ7; NMR; -; A=1-141.
DR   PDB; 2K3F; NMR; -; A=1-141.
DR   PDB; 4V42; X-ray; 5.50 A; BL=1-141.
DR   PDB; 4V4R; X-ray; 5.90 A; BK=1-141.
DR   PDB; 4V4S; X-ray; 6.76 A; BK=1-141.
DR   PDB; 4V4T; X-ray; 6.46 A; BK=1-141.
DR   PDBsum; 1JQM; -.
DR   PDBsum; 1JQS; -.
DR   PDBsum; 1JQT; -.
DR   PDBsum; 1ML5; -.
DR   PDBsum; 1MMS; -.
DR   PDBsum; 1MVR; -.
DR   PDBsum; 1OLN; -.
DR   PDBsum; 1PN7; -.
DR   PDBsum; 1PN8; -.
DR   PDBsum; 1R2W; -.
DR   PDBsum; 1R2X; -.
DR   PDBsum; 2BCW; -.
DR   PDBsum; 2JQ7; -.
DR   PDBsum; 2K3F; -.
DR   PDBsum; 4V42; -.
DR   PDBsum; 4V4R; -.
DR   PDBsum; 4V4S; -.
DR   PDBsum; 4V4T; -.
DR   AlphaFoldDB; P29395; -.
DR   BMRB; P29395; -.
DR   SMR; P29395; -.
DR   IntAct; P29395; 2.
DR   MINT; P29395; -.
DR   STRING; 243274.THEMA_02420; -.
DR   DrugBank; DB02940; (4s)-2-[(1e)-1-Aminoprop-1-Enyl]-4,5-Dihydro-1,3-Thiazole-4-Carboxylic Acid.
DR   DrugBank; DB02566; 8-Hydroxy-4-(1-Hydroxyethyl)Quinoline-2-Carboxylic Acid.
DR   EnsemblBacteria; AAD35537; AAD35537; TM_0454.
DR   KEGG; tma:TM0454; -.
DR   eggNOG; COG0080; Bacteria.
DR   InParanoid; P29395; -.
DR   OMA; CKQFNAK; -.
DR   OrthoDB; 1702697at2; -.
DR   EvolutionaryTrace; P29395; -.
DR   Proteomes; UP000008183; 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: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; Methylation; Reference proteome; Ribonucleoprotein;
KW   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_0000104397"
FT   STRAND          9..14
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   TURN            21..25
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   HELIX           26..29
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   HELIX           35..45
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   STRAND          51..60
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:2JQ7"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   HELIX           75..83
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   TURN            92..94
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   HELIX           102..112
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   HELIX           121..132
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   TURN            133..136
FT                   /evidence="ECO:0007829|PDB:1MMS"
FT   STRAND          137..140
FT                   /evidence="ECO:0007829|PDB:1MMS"
SQ   SEQUENCE   141 AA;  15089 MW;  08AD83D090F651A9 CRC64;
     MAKKVAAQIK LQLPAGKATP APPVGPALGQ HGVNIMEFCK RFNAETADKA GMILPVVITV
     YEDKSFTFII KTPPASFLLK KAAGIEKGSS EPKRKIVGKV TRKQIEEIAK TKMPDLNANS
     LEAAMKIIEG TAKSMGIEVV D
 
 
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