ID EFTU_AZOPC Reviewed; 395 AA.
AC B6YQ04;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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}; OrderedLocusNames=CFPG_013;
OS Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales;
OC Candidatus Azobacteroides.
OX NCBI_TaxID=511995;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19008447; DOI=10.1126/science.1165578;
RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT protist cells in termite gut.";
RL Science 322:1108-1109(2008).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {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}.
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DR EMBL; AP010656; BAG83276.1; -; Genomic_DNA.
DR RefSeq; WP_012573037.1; NC_011565.1.
DR AlphaFoldDB; B6YQ04; -.
DR SMR; B6YQ04; -.
DR STRING; 511995.CFPG_013; -.
DR KEGG; aps:CFPG_013; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_0_10; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000000723; 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; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR CDD; cd03707; EFTU_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00118_B; EF_Tu_B; 1.
DR InterPro; IPR041709; EF-Tu_GTP-bd.
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; T_Tr_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 NCBIfam; TIGR00485; EF-Tu; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..395
FT /note="Elongation factor Tu"
FT /id="PRO_1000095048"
FT DOMAIN 10..204
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 60..64
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 81..84
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 136..139
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 174..176
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 395 AA; 43603 MW; BA7171098F1DA89C CRC64;
MAKEKFNRSK PHVNIGTIGH VDHGKTTLTA AITAVLAKKG LSEVKSFDQI DNAPEEKERG
ITINTAHVEY ETETRHYAHV DCPGHADYVK NMVTGAAQMD GAIIVVAATD GPMPQTREHI
LLARQVNVPK LVVFMNKVDI VDDPEMLELV EMEMRELLDF YQFDGTNTPI IRGSALGGAN
GDPKWEAKIM ELMDAIDNWI PLPQRDIDKS FLMPVEDVFS ITGRGTVATG RIETGLVRTG
DEVQIIGLDA NGKKSVVTGV EMFRKILDEG QAGDNVGLLL RGVDKDEVKR GMVITHPNKV
KPHTKVKAEV YILKKEEGGR HTPFHNKYRP QFYVRTLDVT GEITLPEGTE MVMPGDNVTI
TIELIYPVAC NEGLRFAIRE GGRTVGAGQI TEIIE
//
