Sequences of Escherichia coli uvrA gene and protein reveal two potential ATP binding sites.
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Husain I, Van Houten B, Thomas DC, Sancar A
Sequences of Escherichia coli uvrA gene and protein reveal two potential ATP binding sites.
J Biol Chem. 1986 Apr 15;261(11):4895-901.
- PubMed ID
- 3007478 [ View in PubMed]
- Abstract
We have determined the nucleotide sequence of the uvrA gene of Escherichia coli. The coding region of the gene is 2820 base pairs which specifies a protein of 940 amino acids and Mr = 103,874. The polypeptide sequence predicted from the DNA sequence was confirmed by analyzing the UvrA protein: the sequence of the first 7 NH2-terminal amino acids as well as the amino acid composition of the pure protein agreed with those predicted from the nucleotide sequence. By comparing the sequence of UvrA protein to the amino acid sequences of other ATPases, we found that two regions in the UvrA protein, separated from one another by about 600 amino acids, have the highly conserved G-X4-GKT(S)-X6-I(V) sequence found at the active sites of many, but not all, ATPases. Our findings suggest that UvrA protein may have two ATP binding sites.