(data stored in ACNUC7421 zone)

HOGENOM: BATHU1_1_PE100

ID   BATHU1_1_PE100                       STANDARD;      PRT;   395 AA.
AC   BATHU1_1_PE100; Q6HPR0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Elongation factor Tu; Short=EF-Tu; (BATHU1_1.PE100).
GN   Name=tuf; OrderedLocusNames=BT9727_0104;
OS   BACILLUS THURINGIENSIS SEROVAR KONKUKIAN STR. 97-27.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus
OC   group.
OX   NCBI_TaxID=281309;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BATHU1_1.PE100.
CC       Bacillus thuringiensis serovar konkukian str. 97-27 chromosome, complet
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:EFTU_BACHK
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC       EF-Tu/EF-1A subfamily.
CC   -!- GENE_FAMILY: HOG000229290 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6HPR0; -.
DR   EMBL; AE017355; AAT61478.1; -; Genomic_DNA.
DR   RefSeq; YP_034460.1; NC_005957.1.
DR   HSSP; P0A6N1; 2BVN.
DR   ProteinModelPortal; Q6HPR0; -.
DR   SMR; Q6HPR0; 2-394.
DR   EnsemblBacteria; EBBACT00000076033; EBBACP00000074119; EBBACG00000076024.
DR   GeneID; 2855072; -.
DR   GenomeReviews; AE017355_GR; BT9727_0104.
DR   KEGG; btk:BT9727_0104; -.
DR   GeneTree; EBGT00070000032011; -.
DR   OMA; MEKGLRF; -.
DR   ProtClustDB; PRK00049; -.
DR   BioCyc; BTHU281309:BT9727_0104-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1; -.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   PANTHER; PTHR23115:SF31; Transl_elong_EFTu/EF1A_bac/org; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; Elong_init_C; 1.
DR   SUPFAM; SSF50447; Translat_factor; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS00301; EFACTOR_GTP; 1.
DR   HOGENOMDNA; BATHU1_1.PE100; -.
KW   Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   395 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAKAKFERSK PHVNIGTIGH VDHGKTTLTA AITTVLAKAG GAEARGYDQI DAAPEERERG
     ITISTAHVEY ETETRHYAHV DCPGHADYVK NMITGAAQMD GGILVVSAAD GPMPQTREHI
     LLSRQVGVPY IVVFLNKCDM VDDEELLELV EMEVRDLLSE YGFPGDDIPV IKGSALKALQ
     GEADWEAKII ELMAEVDAYI PTPERETDKP FLMPVEDVFS ITGRGTVATG RVERGIVKVG
     DVVEIIGLAE ENASTTVTGV EMFRKLLDQA QAGDNIGALL RGVAREDIQR GQVLAKSGSV
     KAHAKFKAEV FVLSKEEGGR HTPFFANYRP QFYFRTTDVT GIIQLPEGTE MVMPGDNIEM
     TIELIAPIAI EEGTKFSIRE GGRTVGYGVV ATIVE
//

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