Sequences of Escherichia coli uvrA gene and protein reveal two potential ATP binding sites
- PMID: 3007478
Sequences of Escherichia coli uvrA gene and protein reveal two potential ATP binding sites
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.
Similar articles
-
Both ATPase sites of Escherichia coli UvrA have functional roles in nucleotide excision repair.J Biol Chem. 1991 Jun 15;266(17):11395-403. J Biol Chem. 1991. PMID: 1828249
-
Mutations in the helix-turn-helix motif of the Escherichia coli UvrA protein eliminate its specificity for UV-damaged DNA.J Biol Chem. 1993 Mar 5;268(7):5323-31. J Biol Chem. 1993. PMID: 8444906
-
Deletion mutagenesis of the Escherichia coli UvrA protein localizes domains for DNA binding, damage recognition, and protein-protein interactions.J Biol Chem. 1991 Jun 15;266(17):11388-94. J Biol Chem. 1991. PMID: 1828248
-
Role of ATP hydrolysis by UvrA and UvrB during nucleotide excision repair.Res Microbiol. 2001 Apr-May;152(3-4):401-9. doi: 10.1016/s0923-2508(01)01211-6. Res Microbiol. 2001. PMID: 11421287 Review.
-
The nucleotide excision repair protein UvrB, a helicase-like enzyme with a catch.Mutat Res. 2000 Aug 30;460(3-4):277-300. doi: 10.1016/s0921-8777(00)00032-x. Mutat Res. 2000. PMID: 10946234 Review.
Cited by
-
Molecular genetics of the genus Paracoccus: metabolically versatile bacteria with bioenergetic flexibility.Microbiol Mol Biol Rev. 1998 Dec;62(4):1046-78. doi: 10.1128/MMBR.62.4.1046-1078.1998. Microbiol Mol Biol Rev. 1998. PMID: 9841665 Free PMC article. Review.
-
Amino acid substitution matrices from an information theoretic perspective.J Mol Biol. 1991 Jun 5;219(3):555-65. doi: 10.1016/0022-2836(91)90193-a. J Mol Biol. 1991. PMID: 2051488 Free PMC article.
-
Nucleotide sequence and functional analysis of the RAD1 gene of Saccharomyces cerevisiae.Mol Cell Biol. 1987 Mar;7(3):1012-20. doi: 10.1128/mcb.7.3.1012-1020.1987. Mol Cell Biol. 1987. PMID: 3550428 Free PMC article.
-
Nucleotide sequence and LexA regulation of the Escherichia coli recN gene.Nucleic Acids Res. 1987 Jul 10;15(13):5041-9. doi: 10.1093/nar/15.13.5041. Nucleic Acids Res. 1987. PMID: 3037486 Free PMC article.
-
Nucleotide excision repair in Escherichia coli.Microbiol Rev. 1990 Mar;54(1):18-51. doi: 10.1128/mr.54.1.18-51.1990. Microbiol Rev. 1990. PMID: 2181258 Free PMC article. Review.
Publication types
MeSH terms
Substances
Associated data
- Actions
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases