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PEC Original Annotations
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Essentiality
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Class
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non-essential
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References (PMID)
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Mol Gen Genet. 1999;260(6):603-7.
Either of the chromosomal tuf genes of E. coli K-12 can be deleted without loss of cell viability.
Zuurmond AM, Rundlof AK, Kraal B.
(
9928940
)
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Deletion
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OCL22
(D)
,
OCL22-6
(D)
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Related gene (W3110 PEC)
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Gene Search
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Search MG1655 PEC by gene name:
tufA
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Related strains
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Strains Search
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Search strains by gene name:
tufA
Search strains by all related name:
tufA b3339 ECK3326 f394 JW3301 kirT pulT
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General information (Go to Linear View: )
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Gene Name
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tufA
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Alternative name
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b3339,ECK3326,f394,JW3301,kirT,pulT
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Location, Length
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3,468,167 - 3,469,351
(
-
)
;
74.75
min
;
1185
(bp) ,
394
(aa)
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Product
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protein chain elongation factor EF-Tu (duplicate of tufB)
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Operon Name
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rpsLG-fusA-tufA
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Note
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GO_component: GO:0005737 - cytoplasm; GO_process: GO:0006412 - translation; GO_process: GO:0006970 - response to osmotic stress
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Function
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factor; Proteins - translation and modification
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Gene Ontology
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GO:0000166
;
nucleotide binding ( tufA )
GO:0003746
;
translation elongation factor activity ( tufA )
GO:0003924
;
GTPase activity ( tufA )
GO:0005515
;
protein binding ( tufA )
GO:0005525
;
GTP binding ( tufA )
GO:0005622
;
intracellular ( tufA )
GO:0005737
;
cytoplasm ( tufA )
GO:0005886
;
plasma membrane ( tufA )
GO:0006412
;
translation ( tufA )
GO:0006414
;
translational elongation ( tufA )
GO:0016020
;
membrane ( tufA )
GO:0046677
;
response to antibiotic ( tufA )
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PID
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1789737
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EC number
(KEGG Pathway)
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Verified Protein Starts
(data
compiled from literature and appropriate citations are available from EcoGene)
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EcoGene
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tufA
(
EG11036
)
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Number of removed
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1 aa cleaved
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SWISS-PROT
(
Show simple
)
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Entry name(Acc.no)
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EFTU_ECOLI
(
P02990
;
O68929; Q8X4S9; Q8XED3
)
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- Protein name
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Elongation factor Tu
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- Synonyms
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EF-Tu, P-43
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- Gene name
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Name=tufB; OrderedLocusNames=b3980, c4935, z5553, ECs4903;
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- Comments
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FUNCTION:This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
FUNCTION:May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.
SUBUNIT:Monomer.
SUBCELLULAR LOCATION:Cytoplasmic and membrane-associated.
MISCELLANEOUS:This chain is also used in bacteriophage Q-beta RNA polymerase.
MISCELLANEOUS:The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome.
MISCELLANEOUS:The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu.
MISCELLANEOUS:The sequence of the tufB gene is shown. TufA differs in a single position.
SIMILARITY:Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.
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Homology Analysis
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BLAST
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Bacteria
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GTOP
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tufA
(
homologous genes of other bacterias
)
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PDB
(database updated :
2007.02.20
)
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PSI-BLAST
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Chain G, Whole, Unmodified, Ef-Tu(Elongation Factor Tu).
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SWISS-PROT
(database updated :
2007.02.20
)
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BLAST
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Elongation factor Tu
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PSI-BLAST
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Elongation factor Tu-B
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nr
(database updated :
2007.02.20
)
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BLAST
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elongation factor Tu [Escherichia coli O157:H7 EDL933]
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Pfam 28.0
(database updated :
2015-05
)
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Pfam
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PROSITE
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PROSITE
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ASN_GLYCOSYLATION
GLYCOSAMINOGLYCAN
PKC_PHOSPHO_SITE
CK2_PHOSPHO_SITE
MYRISTYL
ATP_GTP_A
EFACTOR_GTP
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MMBR References
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J Biol Chem. 1996;271:22321-22325
Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli.
Guillon, J. M., S. Heiss, J. Soutourina, Y. Mechulam, S. Laalami, M. Grunberg-Manago, and S. Blanquet.
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Eur J Biochem. 1980;108:507-526
The complete amino-acid sequence of elongation factor Tu from Escherichia coli.
Jones, M. D., T. E. Petersen, K. M. Nielsen, S. Magnusson, L. Sottrup-Jensen, K. Gausing, and B. F. Clark.
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Biochem Cell Biol. 1995;73(11-12):1167-77.
Antibiotic resistance mechanisms of mutant EF-Tu species in Escherichia coli.
Kraal B, Zeef LA, Mesters JR, Boon K, Vorstenbosch EL, Bosch L, Anborgh PH, Parmeggiani A, Hilgenfeld R.
(
8722034
)
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Eur J Biochem. 1987;170:93-98
Molecular cloning and sequence determination of the tuf gene coding for the elongation factor Tu of Thermus thermophilus HB8.
Kushiro, M., M. Shimizu, and K. Tomita.
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J Biol Chem. 1981;256:8102-8109
The amino acid sequence of elongation factor Tu of Escherichia coli. The complete sequence.
Laursen, R. A., J. J. L'Italien, S. Nagarkatti, and D. L. Miller.
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Biochem Biophys Res Commun. 1996;225(3):961-7.
Translational activities of EF-Tu [G222D] which cannot be reconciled with the classical scheme of the polypeptide chain elongation cycle.
Talens A, Boon K, Kraal B, Bosch L.
(
8780718
)
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Proc Natl Acad Sci U S A. 1978;75:4470-4473
Mutants of Escherichia coli altered in both genes coding for the elongation factor Tu.
Van de Klundert, J. A., P. H. Van der Meide, P. Van de Putte, and L. Bosch.
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FEBS Lett. 1982;139(2):325-30.
Regulation of the expression of tufA and tufB, the two genes coding for the elongation factor EF-Tu in Escherichia coli.
van der Meide PH, Vijgenboom E, Dicke M, Bosch L.
(
7042394
)
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J Biol Chem. 1996;271:20406-20411
Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA.
Wiborg, O., C. Andersen, C. R. Knudsen, B. F. C. Clark, and J. Nyborg.
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Gene. 1980;12(1-2):25-31.
The nucleotide sequence of the cloned tufA gene of Escherichia coli.
Yokota T, Sugisaki H, Takanami M, Kaziro Y.
(
7011903
)
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Mol Gen Genet. 1982;185(3):487-92.
A secondary promoter for elongation factor Tu synthesis in the str ribosomal protein operon of Escherichia coli.
Zengel JM, Lindahl L.
(
6285146
)
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J Bacteriol. 1982;149(2):548-53.
Evidence for an internal promoter preceding tufA in the str operon of Escherichia coli.
An G, Lee JS, Friesen JD.
(
6276361
)
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| Sequences |
Amino acid
FASTA format
|
0001 MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG ITINTSHVEY
0071 DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI LLGRQVGVPY IIVFLNKCDM
0141 VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE GDAEWEAKIL ELAGFLDSYI PEPERAIDKP
0211 FLLPIEDVFS ISGRGTVVTG RVERGIIKVG EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR
0281 GIKREEIERG QVLAKPGTIK PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM
0351 VMPGDNIKMV VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLG
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Nucleotide
FASTA format
View sequence out neighbor 100bp
|
-100 caggccgtaa ttgaagcccg tggtaaataa
-070 gcctaagggt taataccaaa gtcccgtgct ctctcctgaa ggggagagca ctatagtaag gaatatagcc
0001 gtgtctaaag aaaaatttga acgtacaaaa ccgcacgtta acgttggtac tatcggccac gttgaccacg
0071 gtaaaactac tctgaccgct gcaatcacca ccgtactggc taaaacctac ggcggtgctg ctcgtgcatt
0141 cgaccagatc gataacgcgc cggaagaaaa agctcgtggt atcaccatca acacttctca cgttgaatac
0211 gacaccccga cccgtcacta cgcacacgta gactgcccgg ggcacgccga ctatgttaaa aacatgatca
0281 ccggtgctgc tcagatggac ggcgcgatcc tggtagttgc tgcgactgac ggcccgatgc cgcagactcg
0351 tgagcacatc ctgctgggtc gtcaggtagg cgttccgtac atcatcgtgt tcctgaacaa atgcgacatg
0421 gttgatgacg aagagctgct ggaactggtt gaaatggaag ttcgtgaact tctgtctcag tacgacttcc
0491 cgggcgacga cactccgatc gttcgtggtt ctgctctgaa agcgctggaa ggcgacgcag agtgggaagc
0561 gaaaatcctg gaactggctg gcttcctgga ttcttatatt ccggaaccag agcgtgcgat tgacaagccg
0631 ttcctgctgc cgatcgaaga cgtattctcc atctccggtc gtggtaccgt tgttaccggt cgtgtagaac
0701 gcggtatcat caaagttggt gaagaagttg aaatcgttgg tatcaaagag actcagaagt ctacctgtac
0771 tggcgttgaa atgttccgca aactgctgga cgaaggccgt gctggtgaga acgtaggtgt tctgctgcgt
0841 ggtatcaaac gtgaagaaat cgaacgtggt caggtactgg ctaagccggg caccatcaag ccgcacacca
0911 agttcgaatc tgaagtgtac attctgtcca aagatgaagg cggccgtcat actccgttct tcaaaggcta
0981 ccgtccgcag ttctacttcc gtactactga cgtgactggt accatcgaac tgccggaagg cgtagagatg
1051 gtaatgccgg gcgacaacat caaaatggtt gttaccctga tccacccgat cgcgatggac gacggtctgc
1121 gtttcgcaat ccgtgaaggc ggccgtaccg ttggcgcggg cgttgttgct aaagttctgg gctaattaca
1191 cgttaattag ttttgaattg aaaagggcgc ttcggcgccc tttttgcatt tgttgacggc atatcttatt
1261 cgtactgtca gaacgaataa attat
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