AC   MF_00118;
DC   Protein; auto
c?   <OC:Bacteria> or <OG:Chloroplast>
TR   HAMAP; MF_00118_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_00118_A; -; 1; level=0
XX
Names: EF_Tu
XX
case <OC:Bacteria>
ID   EFTU
DE   RecName: Full=Elongation factor Tu;
DE            Short=EF-Tu;
GN   Name=tuf;
else case <OC:Archaea>
ID   EF1A
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
DE   AltName: Full=Elongation factor Tu;
DE            Short=EF-Tu;
GN   Name=tuf;
else case <OG:Chloroplast>
ID   EFTU
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
GN   Name=tufA;
end case
XX
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
case <OC:Bacteria>
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
case <OC:Archaea>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
case <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
end case
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily.
XX
DR   Pfam; PF00009; GTP_EFTU; 1; trigger=no
DR   PRINTS; PR00315; ELONGATNFCT; 1; trigger=no
DR   NCBIfam; TIGR00483; EF-1_alpha; 1; trigger=no
DR   NCBIfam; TIGR00485; EF-Tu; 1; trigger=no
DR   PROSITE; PS00301; G_TR_1; 1; trigger=no
DR   PROSITE; PS51722; G_TR_2; 1; trigger=no
XX
case not <OG:Chloroplast>
KW   Cytoplasm
end case
KW   Elongation factor
KW   Protein biosynthesis
KW   GTP-binding
KW   Nucleotide-binding
XX
GO   GO:0005525; F:GTP binding
GO   GO:0003746; F:translation elongation factor activity
case <OC:Bacteria> or <OC:Archaea>
GO   GO:0005737; C:cytoplasm
end case
case <OG:Chloroplast>
GO   GO:0009507; C:chloroplast
end case
XX
FT   From: EFTU1_ECOLI (P0CE47)
case <OC:Bacteria> or <OG:Chloroplast>
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-[HQ]-[IV]-[DY]-H-G-K-[ST]
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: D-x-P-G-H
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: N-K-x-D
end case
FT   From: EF1A_METJA (Q57770)
case <OC:Archaea>
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-H-[IV]-D-[NHA]-G-K-S
FT   BINDING         91..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: D-x-P-G-H
FT   BINDING         149..152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: N-K-M-D
end case
XX
Size: 350-550;
Related: None;
Template: P35021; P0CE47; Q01698; P60338; Q57770;
Scope:
 Bacteria
 Archaea
 Plastid
Fusion:
 Nter: None
 Cter: None
Duplicate: in AQUAE, ECOLI, HAEIN, STRCO, STRRA, THET8
Plasmid: in SHEB5
Comments: Duplicated in some but not necessarily all Acidobacteriota,
 Pseudomonadota, Alkaliohilus, Clostrium, Chloroflexota, Deinococcus,
 Magnetococcus, Sphingobacter, Streptomyces, Syntrophobacter.
 Short versions in EHRRW, VIBVU, and a divergent copy in CHAGL are atypical.
XX
# Revision 1.46 2023/06/01
//