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Database: UniProt/TrEMBL
Entry: F6CKI8_DESK7
LinkDB: F6CKI8_DESK7
Original site: F6CKI8_DESK7 
ID   F6CKI8_DESK7            Unreviewed;       400 AA.
AC   F6CKI8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   22-NOV-2017, entry version 43.
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=Desku_3059 {ECO:0000313|EMBL:AEG16555.1};
OS   Desulfotomaculum kuznetsovii (strain DSM 6115 / VKM B-1805 / 17).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=760568 {ECO:0000313|EMBL:AEG16555.1, ECO:0000313|Proteomes:UP000009229};
RN   [1] {ECO:0000313|EMBL:AEG16555.1, ECO:0000313|Proteomes:UP000009229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6115 / VKM B-1805 / 17 {ECO:0000313|Proteomes:UP000009229};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Lu M., Saunders E., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Nazina T.,
RA   Ivanova A., Parshina S., Kuever J., Muyzer G., Plugge C., Stams A.,
RA   Woyke T.;
RT   "Complete sequence of Desulfotomaculum kuznetsovii DSM 6115.";
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; CP002770; AEG16555.1; -; Genomic_DNA.
DR   STRING; 760568.Desku_3059; -.
DR   EnsemblBacteria; AEG16555; AEG16555; Desku_3059.
DR   KEGG; dku:Desku_3059; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   KO; K02358; -.
DR   OMA; AIRDMGM; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000009229; 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:UP000009229};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AEG16555.1};
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:UP000009229}.
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;  44236 MW;  01875C2DBAAFF7C7 CRC64;
     MAKAKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLATVG KAQVKKYEEI DNAPEERERG
     ITINTAHVEY ETEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPY IVVYMNKADM VDDAELLELV EMEVRELLST YEFPGDDVPV ITGSALKALE
     CGCGKRECEW CKSIWELMDA VDEYIPTPQR DIDKPFLMPI EDVFSITGRG TVVTGRVERG
     TVKVGDEVEI VGLMEKPKKT VVTGVEMFRK ILDRGEAGDN IGCLLRGIER KEVERGMVLA
     KPGSIKPHTH FSAEVYVLTK EEGGRHTPFF NGYRPQFYFR TTDVTGTITL PEGVEMVMPG
     DNVRLEIKLI TPIAIEEGLR FAIREGGRTV GAGVVTQIIE
//
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