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Database: UniProt/TrEMBL
Entry: A0A1U9K3C1_9BACL
LinkDB: A0A1U9K3C1_9BACL
Original site: A0A1U9K3C1_9BACL 
ID   A0A1U9K3C1_9BACL        Unreviewed;       396 AA.
AC   A0A1U9K3C1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   28-MAR-2018, entry version 7.
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   ORFNames=B0W44_00670 {ECO:0000313|EMBL:AQS54527.1};
OS   Novibacillus thermophilus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Novibacillus.
OX   NCBI_TaxID=1471761 {ECO:0000313|EMBL:AQS54527.1, ECO:0000313|Proteomes:UP000188603};
RN   [1] {ECO:0000313|EMBL:AQS54527.1, ECO:0000313|Proteomes:UP000188603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG-1 {ECO:0000313|EMBL:AQS54527.1,
RC   ECO:0000313|Proteomes:UP000188603};
RX   PubMed=25951858; DOI=10.1099/ijs.0.000306;
RA   Yang G., Chen J., Zhou S.;
RT   "Novibacillus thermophilus gen. nov., sp. nov., a Gram-staining-
RT   negative and moderately thermophilic member of the family
RT   Thermoactinomycetaceae.";
RL   Int. J. Syst. Evol. Microbiol. 65:2591-2597(2015).
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; CP019699; AQS54527.1; -; Genomic_DNA.
DR   KEGG; ntr:B0W44_00670; -.
DR   KO; K02358; -.
DR   Proteomes; UP000188603; 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:UP000188603};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AQS54527.1};
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:UP000188603}.
FT   DOMAIN       10    205       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   396 AA;  43343 MW;  7674B8B6AD6EFC6D CRC64;
     MSKEKFERSK PHVNVGTIGH VDHGKTTLTA AITTVLASKG SGEARGYDQI DNAPEERERG
     ITIATSHVEY ETENRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLSQQVGVSH IVVFLNKCDM VDDEELLELV EMEVRDLLSE YDFPGDDIPV IRGSALKALE
     DPNGEWAKSI HELMEQVDSY IPTPERAVDK DFLMPVEDVF SITGRGTVAT GRVERGTIKV
     GDEVEIVGIK PETNKTVVTG VEMFRKLLDQ AEAGDNIGAL LRGVDRDEVE RGQVLAKPGS
     VNPHTKFSGE VYILTKEEGG RHTPFFNGYR PQFYFRTTDV TGVITLPEGT EMVMPGDNVT
     MDVELIAPIA IEDGTRFAIR EGGRTVGAGV VTKINE
//
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