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Database: UniProt/TrEMBL
Entry: E6SLE6_THEM7
LinkDB: E6SLE6_THEM7
Original site: E6SLE6_THEM7 
ID   E6SLE6_THEM7            Unreviewed;       395 AA.
AC   E6SLE6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   28-MAR-2018, entry version 49.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|HAMAP-Rule:MF_00118, ECO:0000256|RuleBase:RU004061};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=Tmar_2311 {ECO:0000313|EMBL:ADU52388.1};
OS   Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM
OS   10246 / 7p75a).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
OX   NCBI_TaxID=644966 {ECO:0000313|EMBL:ADU52388.1, ECO:0000313|Proteomes:UP000008915};
RN   [1] {ECO:0000313|Proteomes:UP000008915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC   {ECO:0000313|Proteomes:UP000008915};
RX   DOI=10.4056/sigs.1373474;
RA   Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L.,
RA   Pitluck S., Pagani I., Ivanova N., Mavromatis K., Mikhailova N.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA   Jeffries C., Schneider S., Rohde M., Goker M., Pukall R., Woyke T.,
RA   Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA   Klenk H., Detter J.;
RT   "Complete genome sequence of Thermaerobacter marianensis type strain
RT   (7p75aT).";
RL   Stand. Genomic Sci. 3:337-345(2010).
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; CP002344; ADU52388.1; -; Genomic_DNA.
DR   RefSeq; WP_013496683.1; NC_014831.1.
DR   STRING; 644966.Tmar_2311; -.
DR   EnsemblBacteria; ADU52388; ADU52388; Tmar_2311.
DR   KEGG; tmr:Tmar_2311; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   BioCyc; TMAR644966:G1GQN-2358-MONOMER; -.
DR   Proteomes; UP000008915; 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; 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 {ECO:0000313|Proteomes:UP000008915};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ADU52388.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008915}.
FT   DOMAIN       10    204       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   395 AA;  43534 MW;  A52A1834AB9AEE11 CRC64;
     MAKAKFERTK PHVNVGTIGH VDHGKTTLTA AITKVLSKQG KAQFVAYDQI DKAPEERERG
     ITIATAHVEY ETDARHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPY IVVFLNKVDM VDDPELLELV ELEVRELLSQ YDFPGDEVPV IKGSALKALE
     EDPEAEKAIL ELMKAVDEYI PTPQRDVDKP FLMPVEDVFS ITGRGTVATG RVERGRVKVG
     DEVELVGFTD KPRKTVVTGV EMFRKVLDEA VAGDNIGCLL RGMDKDEVER GQVLAKPGSI
     NPHKKFVGNV YVLKKEEGGR HTPFFNGYRP QFYFRTTDVT GEIKLPEGVE MCMPGDNIEM
     TVELITPIAI EEGLRFAIRE GGRTVGAGVV TKILE
//
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