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Database: UniProt/SWISS-PROT
Entry: EFTU_NITWN
LinkDB: EFTU_NITWN
Original site: EFTU_NITWN 
ID   EFTU_NITWN              Reviewed;         396 AA.
AC   Q3SSW8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   05-DEC-2018, entry version 90.
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=Nwi_1362;
OS   Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS   NCIMB 11846 / Nb-255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX   PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006;
RA   Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L.,
RA   Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J.,
RA   Arp D.J., Hickey W.J.;
RT   "Genome sequence of the chemolithoautotrophic nitrite-oxidizing
RT   bacterium Nitrobacter winogradskyi Nb-255.";
RL   Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA04623.1; -; Genomic_DNA.
DR   RefSeq; WP_011314640.1; NC_007406.1.
DR   ProteinModelPortal; Q3SSW8; -.
DR   SMR; Q3SSW8; -.
DR   STRING; 323098.Nwi_1362; -.
DR   PRIDE; Q3SSW8; -.
DR   EnsemblBacteria; ABA04623; ABA04623; Nwi_1362.
DR   KEGG; nwi:Nwi_1362; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   BioCyc; NWIN323098:G1G55-1389-MONOMER; -.
DR   Proteomes; UP000002531; 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; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    396       Elongation factor Tu.
FT                                /FTId=PRO_1000015713.
FT   DOMAIN       10    206       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   396 AA;  43180 MW;  149E73F45CDD765D CRC64;
     MAKAKFERNK PHCNIGTIGH VDHGKTSLTA AITKVLAEAG GATFTAYDQI DKAPEEKARG
     ITISTSHVEY ETPNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA IVVFLNKCDM VDDPELLELV EMEVRELLSK YEFPGDDIPI IKGSALAALE
     DSDAKLGKEA VLELMKAVDA YIPQPERPVD QPFLMPVEDV FSISGRGTVV TGRVERGIVK
     VGEEIEIVGI RETQKTTVTG VEMFRKLLDQ GQAGDNIGAL LRGTKREDVE RGQVLCKPGS
     VKPHTKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVVHLPAGT EMVMPGDNVA
     MEVHLIVPIA MEEKLRFAIR EGGRTVGAGV VASIIE
//
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