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Database: UniProt/TrEMBL
Entry: F6BGH0_THEXL
LinkDB: F6BGH0_THEXL
Original site: F6BGH0_THEXL 
ID   F6BGH0_THEXL            Unreviewed;       400 AA.
AC   F6BGH0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-SEP-2017, entry version 42.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=Thexy_0332 {ECO:0000313|EMBL:AEF16388.1};
OS   Thermoanaerobacterium xylanolyticum (strain ATCC 49914 / DSM 7097 /
OS   LX-11).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Thermoanaerobacterium.
OX   NCBI_TaxID=858215 {ECO:0000313|EMBL:AEF16388.1, ECO:0000313|Proteomes:UP000007239};
RN   [1] {ECO:0000313|Proteomes:UP000007239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Hemme C., Woyke T.;
RT   "Complete sequence of Thermoanaerobacterium xylanolyticum LX-11.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00118}.
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DR   EMBL; CP002739; AEF16388.1; -; Genomic_DNA.
DR   RefSeq; WP_013787148.1; NC_015555.1.
DR   STRING; 858215.Thexy_0332; -.
DR   PRIDE; F6BGH0; -.
DR   EnsemblBacteria; AEF16388; AEF16388; Thexy_0332.
DR   KEGG; txy:Thexy_0332; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000007239; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03697; EFTU_II; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007239};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AEF16388.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   DOMAIN       10    209       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      19     26       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
SQ   SEQUENCE   400 AA;  44027 MW;  AAD559988B3471DA CRC64;
     MAKQKFERKK PHANIGTIGH VDHGKTTLTS AITIVLSKQG MAQATAYDEI DKAPEEKARG
     ITINTMHVEY ETEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPY IVVFLNKADM VDDQELIELV EMEVRELLNE YEFPGDDTPI VVGSALKAME
     CGCGQRDCQW CGKIWDLMDA VDSYIPTPER DVDKPFLMPV EDVFTITGRG TVATGRVERG
     KLKVGDEVEI IGLSDESKKT VVTGVEMFRK TLDEAEAGDN IGVLLRGVTR EEVERGQVLA
     KPGSVKPHTK FEGQVYVLTK EEGGRHTPFF NGYRPQFYFR TTDVTGVIEL PEGVEMVMPG
     DHVTMTIELI TPIAMEEGLK FAIREGGHTV GAGVVSKILA
//
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