ID EFTU_GRABC Reviewed; 396 AA.
AC Q0BUQ2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 16-JAN-2019, entry version 84.
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=GbCGDNIH1_0552;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K.,
RA Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W.,
RA Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI61450.1; -; Genomic_DNA.
DR RefSeq; WP_011631260.1; NC_008343.2.
DR ProteinModelPortal; Q0BUQ2; -.
DR SMR; Q0BUQ2; -.
DR STRING; 391165.GbCGDNIH1_0552; -.
DR PRIDE; Q0BUQ2; -.
DR EnsemblBacteria; ABI61450; ABI61450; GbCGDNIH1_0552.
DR GeneID; 31475255; -.
DR KEGG; gbe:GbCGDNIH1_0552; -.
DR eggNOG; ENOG4105CGV; Bacteria.
DR eggNOG; COG0050; LUCA.
DR HOGENOM; HOG000229290; -.
DR KO; K02358; -.
DR OMA; YGHIDCP; -.
DR BioCyc; GBET391165:G1G6T-564-MONOMER; -.
DR Proteomes; UP000001963; 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_1000015669.
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; 43008 MW; E5CAB22B0312B606 CRC64;
MAKAKFERNK PHCNIGTIGH VDHGKTSLTA AITKVLAETG GATFTAYDQI DKAPEERARG
ITISTAHVEY ETGNRHYAHV DCPGHADYVK NMITGAAQMD GGILVVSAAD GPMPQTREHI
LLARQVGVPA LVVFLNKVDM VDDPELLDLV EMEVRELLSS YQFPGDDIPI IKGSALCALE
DKNPEIGRDA ILKLMEAVDA YIPQPERPLD RPFLMPIEDV FSISGRGTVV TGRIERGEVK
VGDEVEIVGL KATSKTTVTG VEMFRKLLDR GEAGDNIGAL LRGTKREDVE RGQVLAKPGS
ITPHTKFAAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVVSLPEGT EMVMPGDNVS
MQVELIAPIA MDEGLRFAIR EGGRTVGAGV VAKISQ
//
