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Database: UniProt/TrEMBL
Entry: W0HFU6_PSECI
LinkDB: W0HFU6_PSECI
Original site: W0HFU6_PSECI 
ID   W0HFU6_PSECI            Unreviewed;       397 AA.
AC   W0HFU6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-SEP-2017, entry version 22.
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=PCH70_45770 {ECO:0000313|EMBL:AHF69730.1};
OS   Pseudomonas cichorii JBC1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1441629 {ECO:0000313|EMBL:AHF69730.1, ECO:0000313|Proteomes:UP000019031};
RN   [1] {ECO:0000313|EMBL:AHF69730.1, ECO:0000313|Proteomes:UP000019031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBC1 {ECO:0000313|EMBL:AHF69730.1,
RC   ECO:0000313|Proteomes:UP000019031};
RA   Kim B.-Y., Lee Y.H.;
RT   "Analysis of whole genome sequence of Pseudomonas cichorii JBC1.";
RL   Submitted (JAN-2014) 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; CP007039; AHF69730.1; -; Genomic_DNA.
DR   RefSeq; WP_025262054.1; NZ_CP007039.1.
DR   EnsemblBacteria; AHF69730; AHF69730; PCH70_45770.
DR   KEGG; pci:PCH70_45770; -.
DR   PATRIC; fig|1441629.3.peg.4504; -.
DR   KO; K02358; -.
DR   Proteomes; UP000019031; 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.
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:UP000019031};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118};
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}.
FT   DOMAIN       10    207       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   397 AA;  43454 MW;  FCDC2E87305EF306 CRC64;
     MAKEKFERNK PHVNVGTIGH VDHGKTTLTA ALTRVCSEVF GSAKVDFDKI DSAPEEKARG
     ITINTAHVEY DSSVRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
     LLSRQVGVPY IVVFLNKADM VDDAELLELV EMEVRDLLST YDFPGDDTPI IIGSALMALN
     GQDDNEMGTS AVKKLVETLD SYIPEPERAI DKPFLMPIED VFSISGRGTV VTGRVERGII
     KIQEEVEIVG LRDTTKTTCT GVEMFRKLLD EGRAGENCGV LLRGTKRDDV ERGQVLVKPG
     TVKPHTQFEA EIYVLSKEEG GRHTPFFKGY RPQFYFRTTD VTGSCELPEG VEMVMPGDNV
     KVSVTLIKPI AMEDGLRFAI REGGRTVGAG VVAKIIA
//
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