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HAMAP annotation rule: MF_00118
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General rule information

Accession MF_00118
Dates 1-JUN-2001 (Created)
12-FEB-2010 (Last updated, Version 36)
Data class Protein

case <OC:Bacteria> or <OG:Chloroplast>
Predictors HAMAP; MF_00118_B; [distribution of match scores in UniProtKB];[seed alignment for MF_00118_B]
end case


case <OC:Archaea>
Predictors HAMAP; MF_00118_A; [distribution of match scores in UniProtKB];[seed alignment for MF_00118_A]
end case

Names EF_Tu


Propagated annotation

Identifier, protein and gene names

case <OC:Bacteria>
Identifier EFTU
Protein name
RecName: Full=Elongation factor Tu;
Short=EF-Tu;
Gene name tuf

else case <OC:Archaea>
Identifier EF1A
Protein name
RecName: Full=Elongation factor 1-alpha;
Short=EF-1-alpha;
AltName: Full=Elongation factor Tu;
Short=EF-Tu;
Gene name tuf

else case <OG:Chloroplast>
Identifier EFTU
Protein name
RecName: Full=Elongation factor Tu, chloroplastic;
Short=EF-Tu;
Gene name tufA
end case

Comments
FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity).

case <OC:Bacteria>
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
end case


case <OC:Archaea>
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
end case


case <OG:Chloroplast>
SUBCELLULAR LOCATION: Plastid, chloroplast.
end case

SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.
Cross-references
Pfam PF00009; GTP_EFTU; 1;
PRINTS PR00315; ELONGATNFCT; 1;
TIGRFAMs TIGR00483; EF-1_alpha; 1;
TIGR00485; EF-Tu; 1;
PROSITE PS00301; EFACTOR_GTP; 1;
Keywords

case <FT:4>
Acetylation.
end case


case not <OG:Chloroplast>
Cytoplasm.
end case

Elongation factor, Protein biosynthesis, GTP-binding, Nucleotide-binding.
Gene Ontology
GO:0005525; Molecular function: GTP binding.
GO:0003746; Molecular function: translation elongation factor activity.

case <OC:Bacteria> or <OC:Archaea>
GO:0005737; Cellular component: cytoplasm.
end case


case <OG:Chloroplast>
GO:0009507; Cellular component: chloroplast.
end case

Features

case <OC:Bacteria> or <OG:Chloroplast>
From: EFTU1_ECOLI (P0CE47)
Key     From     To       Description   Condition   FTGroup
NP_BIND     19     26       GTP (By similarity)   G-[HQ]-[IV]-[DY]-H-G-K-[ST]  
NP_BIND     81     85       GTP (By similarity)   D-x-P-G-H  
NP_BIND     136     139       GTP (By similarity)   N-K-x-D  
end case

case <OC:Escherichia> or <OC:Shigella>
Key     From     To       Description   Condition   FTGroup
MOD_RES     314     314       N6-acetyllysine (By similarity)   K  
end case

case <OC:Archaea>
From: EF1A_METJA (Q57770)
Key     From     To       Description   Condition   FTGroup
NP_BIND     14     21       GTP (By similarity)   G-H-[IV]-D-[NHA]-G-K-S  
NP_BIND     91     95       GTP (By similarity)   D-x-P-G-H  
NP_BIND     149     152       GTP (By similarity)   N-K-M-D  
end case



Additional information


case <OC:Bacteria>
Size range: 389-430 amino acids
end case


case <OC:Archaea>
Size range: 413-444 amino acids
end case

Related UniRules: None
Template: P35021 (EF1A_SULSO); P0CE47 (EFTU1_ECOLI); Q01698 (EFTU_THEAQ); P60338 (EFTU1_THETH); Q57770 (EF1A_METJA): [Recover all]
Scope: Bacteria
Archaea
Plastid
Fusion: Nter: None; Cter: None
Duplicate: in AQUAE, ECOLI, HAEIN, STRCO, STRRA, THET8
Plasmid encoded: in SHEB5
Comments: Duplicated in some but not necessarily all Acidobacteria, Proteobacteria, Alkaliohilus, Clostrium, Chloroflexi, Deinococcus, Magnetococcus, Sphingobacter, Streptomyces, Syntrophobacter. Short versions in EHRRW, VIBVU, and a divergent copy in CHAGL are atypical.

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UniProtKB rule member sequences