ID EFTU_GLUDA Reviewed; 396 AA.
AC A9H3R7; B5ZIG1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 28-FEB-2018, entry version 71.
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=GDI3406, Gdia_2964;
OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 /
OS PAl5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=272568;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / PAl5;
RX PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A.,
RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L.,
RA Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M.,
RA Nogueira E., Cidade D., Oliveira D., Simao T., Macedo J., Valadao A.,
RA Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E.,
RA Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H.,
RA Junior J., de Souza Filho G., Martin Quintana Flores V., Ferreira B.,
RA Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J.,
RA Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E.,
RA Amaral G., Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P.,
RA Rossle S.C., Urmenyi T., Rael Pereira A., Silva R., Rondinelli E.,
RA von Kruger W., Martins O., Baldani J.I., Ferreira P.C.;
RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT Gluconacetobacter diazotrophicus Pal5.";
RL BMC Genomics 10:450-450(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / PAl5;
RX PubMed=21304715; DOI=10.4056/sigs.972221;
RA Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.;
RT "Two genome sequences of the same bacterial strain, Gluconacetobacter
RT diazotrophicus PAl 5, suggest a new standard in genome sequence
RT submission.";
RL Stand. Genomic Sci. 2:309-317(2010).
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; AM889285; CAP57349.1; -; Genomic_DNA.
DR EMBL; CP001189; ACI52694.1; -; Genomic_DNA.
DR RefSeq; WP_012227963.1; NC_011365.1.
DR ProteinModelPortal; A9H3R7; -.
DR SMR; A9H3R7; -.
DR STRING; 272568.Gdia_2964; -.
DR PRIDE; A9H3R7; -.
DR EnsemblBacteria; ACI52694; ACI52694; Gdia_2964.
DR EnsemblBacteria; CAP57349; CAP57349; GDI3406.
DR KEGG; gdi:GDI3406; -.
DR KEGG; gdj:Gdia_2964; -.
DR eggNOG; ENOG4105CGV; Bacteria.
DR eggNOG; COG0050; LUCA.
DR HOGENOM; HOG000229290; -.
DR KO; K02358; -.
DR OMA; YGHIDCP; -.
DR OrthoDB; POG091H00LA; -.
DR BioCyc; GDIA272568:G1GTW-3010-MONOMER; -.
DR Proteomes; UP000000736; Chromosome.
DR Proteomes; UP000001176; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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_1000076099.
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; 43009 MW; F6898013586E022D CRC64;
MAKAKFERTK PHCNIGTIGH VDHGKTSLTA AITKTLAKTG GATFKAYDQI DAAPEERARG
ITISTAHVEY ETAKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
LLARQVGVPA LVVFLNKVDQ VDDPELLELV EMEVRELLSA YQFPGDDIPI IKGSALVTLE
DGDPEVGENR VRDLMDAVDA YIPQPERPVD RPFLMPIEDV FSISGRGTVV TGRVERGVVN
VGDEIEIVGL RATQKTTVTG VEMFRKLLDR GEAGDNIGAL VRGTKREDVE RGQVLAKPGS
ITPHTKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVVHLPEGT EMVMPGDNIA
MDVELIAPIA MDEGLRFAIR EGGRTVGAGV VASITA
//
