Reviewed,
UniProtKB/Swiss-Prot P0A6N3 (EFTU_ECO57)
Last modified
November 24, 2009.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Elongation factor Tu Short name=EF-Tu Alternative name(s): P-43 | |||||||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | |||||||||
| Taxonomic identifier | 83334 [NCBI] | |||||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 394 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis By similarity. May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation By similarity. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm. Cell membrane; Peripheral membrane protein By similarity. |
| Miscellaneous | This chain is also used in bacteriophage Q-beta RNA polymerase By similarity. The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome By similarity. The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu By similarity. The sequence of the tufB gene is shown. TufA differs in a single position By similarity. |
| Sequence similarities | Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic resistance Protein biosynthesis |
| Cellular component | Cell membrane Cytoplasm Membrane |
| Ligand | GTP-binding Nucleotide-binding |
| Molecular function | Elongation factor |
| PTM | Acetylation Methylation Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW translational elongationInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membraneInferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activityInferred from electronic annotation. Source: InterPro translation elongation factor activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 394 | 393 | Elongation factor Tu HAMAP MF_00118 | PRO_0000091321 | |||||
Regions | |||||||||
| Nucleotide binding | 19 – 26 | 8 | GTP By similarity | ||||||
| Nucleotide binding | 81 – 85 | 5 | GTP By similarity | ||||||
| Nucleotide binding | 136 – 139 | 4 | GTP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 57 | 1 | N6-methylated lysine By similarity | ||||||
| Modified residue | 314 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 383 | 1 | Phosphothreonine By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 394 | 1 | S → G in tufA. | ||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG58446.1. AE005174 Genomic DNA. Translation: AAG59176.1. BA000007 Genomic DNA. Translation: BAB37613.1. BA000007 Genomic DNA. Translation: BAB38326.1. | |
| PIR | B85998. G91241. |
| RefSeq | NP_289886.1. NP_290611.1. NP_312217.1. NP_312930.1. |
3D structure databases | |
| SMR | P0A6N3. Positions 9-394. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P0A6N3. |
Genome annotation databases | |
| GeneID | 914959. 915957. 958801. 960150. |
| GenomeReviews | Gene locus Z4697 in contig AE005174_GR. Gene locus Z5553 in contig AE005174_GR. Gene locus ECs4190 in contig BA000007_GR. Gene locus ECs4903 in contig BA000007_GR. |
| KEGG | ece:Z4697. ece:Z5553. ecs:ECs4190. ecs:ECs4903. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0A6N3. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS4190-MON. ECOL83334:ECS4903-MON. |
Family and domain databases | |
| HAMAP | MF_00118. [Tree] |
| InterPro | IPR000795. ProtSyn_GTP_bd. IPR005225. Small_GTP_bd. IPR009001. Transl_elong_EF1A/Init_IF2_C. IPR004161. Transl_elong_EFTu/EF1A_2. IPR004541. Transl_elong_EFTu/EF1A_bac/org. IPR004160. Transl_elong_EFTu/EF1A_C. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view] |
| PANTHER | PTHR23115:SF31. Transl_elong_EFTu/EF1A_bac/org. 1 hit. |
| Pfam | PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. PF03143. GTP_EFTU_D3. 1 hit. [Graphical view] |
| PRINTS | PR00315. ELONGATNFCT. |
| TIGRFAMs | TIGR00485. EF-Tu. 1 hit. TIGR00231. small_GTP. 1 hit. |
| PROSITE | PS00301. EFACTOR_GTP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | EFTU_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0A6N3 Secondary accession number(s): O68929 Q8XED3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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