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Database: UniProt/TrEMBL
Entry: F6AJ92_PSEF1
LinkDB: F6AJ92_PSEF1
Original site: F6AJ92_PSEF1 
ID   F6AJ92_PSEF1            Unreviewed;       397 AA.
AC   F6AJ92;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   22-NOV-2017, entry version 42.
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=Psefu_0626 {ECO:0000313|EMBL:AEF20604.1}, Psefu_0638
GN   {ECO:0000313|EMBL:AEF20616.1};
OS   Pseudomonas fulva (strain 12-X).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF20604.1, ECO:0000313|Proteomes:UP000000686};
RN   [1] {ECO:0000313|EMBL:AEF20604.1, ECO:0000313|Proteomes:UP000000686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA   Woyke T.;
RT   "Complete sequence of Pseudomonas fulva 12-X.";
RL   Submitted (APR-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; CP002727; AEF20604.1; -; Genomic_DNA.
DR   EMBL; CP002727; AEF20616.1; -; Genomic_DNA.
DR   RefSeq; WP_013789746.1; NC_015556.1.
DR   STRING; 743720.Psefu_0638; -.
DR   EnsemblBacteria; AEF20604; AEF20604; Psefu_0626.
DR   EnsemblBacteria; AEF20616; AEF20616; Psefu_0638.
DR   GeneID; 31808440; -.
DR   KEGG; pfv:Psefu_0626; -.
DR   KEGG; pfv:Psefu_0638; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000000686; 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:UP000000686};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AEF20604.1};
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:UP000000686}.
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;  43579 MW;  8CDC91D9135259CB CRC64;
     MAKEKFERNK PHVNVGTIGH VDHGKTTLTA ALTRVCSEVF GSARVDFDKI DSAPEEKARG
     ITINTAHVEY DSNIRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
     LLSRQVGVPY IVVFLNKADM VDDAELLELV EMEVRDLLST YDFPGDDTPI IIGSALMALN
     GQDDNEMGTT AVKKLVETLD TYIPEPVRAI DRPFLMPIED VFSISGRGTV VTGRVERGIV
     KIQEEIEIVG LRATTKTTCT GVEMFRKLLD EGRAGENCGV LLRGTKRDDV ERGQVLAKPG
     TIKPHTKFEA EVYVLSKEEG GRHTPFFKGY RPQFYFRTTD VTGSCELPEG VEMVMPGDNI
     KMVVTLIKPI AMEDGLRFAI REGGRTVGAG VVAKIVE
//
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