Elongation factor Tu - Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

Contribute

Send feedback

Read comments (?) or add your own

P0A6N2 (EFTU_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Elongation factor Tu
Short name=EF-Tu

Alternative name(s):
P-43

Gene names

Name:	tufA
Ordered Locus Names:	c4111
AND
Name:	tufB
Ordered Locus Names:	c4935

Organism

Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

199310 [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. HAMAP-Rule MF_00118_B May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation By similarity. HAMAP-Rule MF_00118_B
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm. Cell inner membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_00118_B.
Miscellaneous	This chain is also used in bacteriophage Q-beta RNA polymerase By similarity. HAMAP-Rule MF_00118_B The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome By similarity. HAMAP-Rule MF_00118_B The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu By similarity. HAMAP-Rule MF_00118_B The sequence of the tufB gene is shown. TufA differs in a single position By similarity. HAMAP-Rule MF_00118_B
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.
Sequence caution	The sequence AAN82549.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Antibiotic resistance Protein biosynthesis
Cellular component	Cell inner membrane 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	GTP catabolic process Inferred from electronic annotation. Source: GOC response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activity Inferred from electronic annotation. Source: InterPro translation elongation factor activity Inferred 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

Removed By similarity

Chain

2 – 394

393

Elongation factor Tu HAMAP-Rule MF_00118_B

PRO_0000091322

Regions

Nucleotide binding

19 – 26

GTP By similarity

Nucleotide binding

81 – 85

GTP By similarity

Nucleotide binding

136 – 139

GTP By similarity

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

N6-methylated lysine By similarity

Modified residue

314

N6-acetyllysine By similarity

Modified residue

383

Phosphothreonine By similarity

Natural variations

Natural variant

394

S → G in tufA.

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6N2 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6EDA60255F43358F
Show »

FASTA

394

43,314

        10         20         30         40         50         60 
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG 

        70         80         90        100        110        120 
ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI 

       130        140        150        160        170        180 
LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE 

       190        200        210        220        230        240 
GDAEWEAKIL ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG 

       250        260        270        280        290        300 
EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK 

       310        320        330        340        350        360 
PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV 

       370        380        390 
VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLS

« Hide

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TUFA AND TUFB).
Strain: CFT073 / ATCC 700928 / UPEC.

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN82549.1. Different initiation. AE014075 Genomic DNA. Translation: AAN83363.1.
RefSeq	NP_755975.2. NC_004431.1. NP_756789.1. NC_004431.1.
3D structure databases
ProteinModelPortal	P0A6N2.
SMR	P0A6N2. Positions 9-394.
ModBase	Search...
Protein-protein interaction databases
STRING	199310.c4111.
Proteomic databases
PRIDE	P0A6N2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN82549; AAN82549; c4111. AAN83363; AAN83363; c4935.
GeneID	1036191. 1039881.
KEGG	ecc:c4111. ecc:c4935.
PATRIC	18285976. VBIEscCol75197_3864.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000229290.
KO	K02358.
OMA	CEFVGYN.
ProtClustDB	PRK12735.
Family and domain databases
HAMAP	MF_00118_B. EF_Tu_B.
InterPro	IPR000795. EF_GTP-bd_dom. IPR005225. Small_GTP-bd_dom. 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]
Pfam	PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. PF03143. GTP_EFTU_D3. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
SUPFAM	SSF50465. Elong_init_C. 1 hit. SSF50447. Translat_factor. 1 hit.
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_ECOL6

Accession

Primary (citable) accession number: P0A6N2
Secondary accession number(s): O68929

Q8XED3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents