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Database: UniProt/SWISS-PROT
Entry: EFTU_CALBD
LinkDB: EFTU_CALBD
Original site: EFTU_CALBD 
ID   EFTU_CALBD              Reviewed;         400 AA.
AC   B9MQH1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   22-NOV-2017, entry version 58.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=Athe_0810;
OS   Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
OS   (Anaerocellum thermophilum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Caldicellulosiruptor.
OX   NCBI_TaxID=521460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Kataeva I., Adams M.W.W.;
RT   "Complete sequence of chromosome of Anaerocellum thermophilum DSM
RT   6725.";
RL   Submitted (JAN-2009) 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:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00118}.
DR   EMBL; CP001393; ACM59925.1; -; Genomic_DNA.
DR   RefSeq; WP_013403741.1; NC_012034.1.
DR   ProteinModelPortal; B9MQH1; -.
DR   SMR; B9MQH1; -.
DR   STRING; 521460.Athe_0810; -.
DR   PRIDE; B9MQH1; -.
DR   EnsemblBacteria; ACM59925; ACM59925; Athe_0810.
DR   GeneID; 31772165; -.
DR   KEGG; ate:Athe_0810; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; AIRDMGM; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000007723; Chromosome.
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   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; IPR031157; G_TR_CS.
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_sf.
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; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    400       Elongation factor Tu.
FT                                /FTId=PRO_1000201376.
FT   DOMAIN       10    209       tr-type G.
FT   NP_BIND      19     26       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   REGION       19     26       G1. {ECO:0000250}.
FT   REGION       60     64       G2. {ECO:0000250}.
FT   REGION       81     84       G3. {ECO:0000250}.
FT   REGION      136    139       G4. {ECO:0000250}.
FT   REGION      174    176       G5. {ECO:0000250}.
SQ   SEQUENCE   400 AA;  44008 MW;  2F1372E372AA7632 CRC64;
     MAKAKFERTK PHVNIGTIGH VDHGKTTLTA AITKVLALKG KAQFMAYDQI DKAPEERERG
     ITINTAHVEY ETDARHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVNVPY IVVFLNKVDM VDDPELIELV EMEVRELLSK YGYPGDEVPI VKGSALKALE
     STSQDPNAPE YQCILELMDA VDKYIPTPQR DIDKPFLMPI EDVFSITGRG TVVTGRVERG
     TLKTGEEVEI VGFAPEPRKT VVTGIEMFRK VLDEAVAGDN VGCLLRGIQK NEVERGQVLA
     KPGTIKPHTK FKAQVYVLTK EEGGRHTPFF NGYRPQFYFR TTDVTGTITL PEGVEMCMPG
     DNVEMTVELI SPIAIESGLR FAIREGGRTV GAGSVTTIIE
//
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