Identification
Name:ATP-dependent DNA helicase rep
Synonyms:Not Available
Gene Name:rep
Enzyme Class:
Biological Properties
General Function:Replication, recombination and repair
Specific Function:Rep helicase is a single-stranded DNA-dependent ATPase involved in DNA replication; it can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3' to 5' direction
Cellular Location:Cytoplasmic
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
ATP-dependent DNA helicase activity
binding
catalytic activity
DNA binding
DNA helicase activity
helicase activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
nucleic acid binding
nucleoside binding
nucleoside-triphosphatase activity
purine nucleoside binding
pyrophosphatase activity
Process
cellular macromolecule metabolic process
cellular process
DNA conformation change
DNA duplex unwinding
DNA geometric change
DNA metabolic process
DNA repair
DNA unwinding involved in replication
macromolecule metabolic process
metabolic process
Gene Properties
Blattner:Not Available
Gene OrientationNot Available
Centisome Percentage:Not Available
Left Sequence EndNot Available
Right Sequence EndNot Available
Gene Sequence:
>2022 bp
ATGCGTCTAAACCCCGGCCAACAACAAGCTGTCGAATTCGTTACCGGCCCCTGCCTGGTG
CTGGCGGGCGCGGGTTCCGGTAAAACTCGTGTTATCACCAATAAAATCGCCCATCTGATC
CGCGGTTGCGGTTATCAGGCGCGGCACATTGCGGCGGTGACCTTTACTAATAAAGCAGCG
CGCGAGATGAAAGAGCGTGTAGGGCAGACGCTGGGGCGCAAAGAGGCGCGTGGGCTGATG
ATCTCCACTTTCCATACGTTGGGGCTGGATATCATCAAACGCGAGTATGCGGCGCTTGGG
ATGAAAGCGAACTTCTCGTTGTTTGACGATACCGATCAGCTTGCTTTGCTTAAAGAGTTG
ACCGAGGGGCTGATTGAAGATGACAAAGTTCTCCTGCAACAACTGATTTCGACCATCTCT
AACTGGAAGAATGATCTCAAAACACCGTCCCAGGCGGCAGCAAGTGCGATTGGCGAGCGG
GACCGTATTTTTGCCCATTGTTATGGGCTGTATGATGCACACCTGAAAGCCTGTAACGTT
CTCGACTTCGATGATCTGATTTTATTGCCGACGTTGCTGCTGCAAGCCAATGAAGAAGTC
CGCAAGCGCTGGCAGAACAAAATTCGCTATCTGCTGGTGGATGAGTATCAGGACACCAAC
ACCAGCCAGTATGAGCTGGTGAAACTGCTGGTGGGCAGCCGCGCGCGCTTTACCGTGGTG
GGTGACGATGACCAGTCGATCTACTCCTGGCGCGGTGCACGTCCGCAAAACCTGGTGCTG
CTGAGTCAGGATTTTCCGGCGCTGAAGGTGATTAAGCTTGAGCAGAACTATCGCTCTTCC
GGGCGTATTCTGAAAGCGGCGAACATCCTGATCGCCAATAACCCGCACGTCTTTGAAAAG
CGTCTGTTCTCCGAACTGGGTTATGGCGCGGAGCTAAAAGTATTAAGCGCGAATAACGAA
GAACATGAGGCTGAGCGCGTTACTGGCGAGCTGATCGCCCATCACTTCGTCAATAAAACG
CAGTACAAAGATTACGCCATTCTTTATCGCGGTAACCATCAGTCGCGGGTGTTTGAAAAA
TTCCTGATGCAAAACCGCATCCCGTACAAAATATCTGGTGGTACGTCGTTTTTCTCTCGT
CCTGAAATCAAGGACTTGCTGGCTTATCTGCGCGTGCTGACTAACCCGGACGATGACAGC
GCATTTCTGCGTATCGTTAACACGCCGAAGCGAGAGATTGGCCCGGCTACGCTGAAAAAG
CTGGGTGAGTGGGCGATGACGCGCAATAAAAGCATGTTTACCGCCAGCTTTGATATGGGC
CTGAGTCAGACGCTTAGCGGACGTGGTTATGAAGCATTGACCCGCTTCACTCACTGGTTG
GCAGAAATCCAGCGTCTGGCGGAGCGGGAGCCGATTGCCGCGGTGCGTGATCTGATCCAT
GGCATGGATTATGAATCCTGGCTGTACGAAACATCGCCCAGCCCGAAAGCCGCCGAAATG
CGCATGAAGAACGTCAACCAACTGTTTAGCTGGATGACGGAGATGCTGGAAGGCAGTGAA
CTGGATGAGCCGATGACGCTCACCCAGGTGGTGACGCGCTTTACTTTGCGCGACATGATG
GAGCGTGGTGAGAGTGAAGAAGAGCTGGATCAGGTGCAACTGATGACTCTCCACGCGTCG
AAAGGGCTGGAGTTTCCTTATGTCTACATGGTCGGTATGGAAGAAGGGTTTTTGCCGCAC
CAGAGCAGCATCGATGAAGATAATATCGATGAGGAGCGGCGGCTGGCCTATGTCGGCATT
ACCCGCGCCCAGAAGGAATTGACCTTTACGCTGTGTAAAGAACGCCGTCAGTACGGCGAA
CTGGTGCGCCCGGAGCCGAGCCGCTTTTTGCTGGAGCTGCCGCAGGATGATCTGATTTGG
GAACAGGAGCGCAAAGTGGTCAGCGCCGAAGAACGGATGCAGAAAGGGCAAAGCCATCTG
GCGAATCTGAAAGCGATGATGGCGGCAAAACGAGGGAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:673
Protein Molecular Weight:77024
Protein Theoretical pI:7
PDB File:1UAA
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>ATP-dependent DNA helicase rep
MRLNPGQQQAVEFVTGPCLVLAGAGSGKTRVITNKIAHLIRGCGYQARHIAAVTFTNKAA
REMKERVGQTLGRKEARGLMISTFHTLGLDIIKREYAALGMKANFSLFDDTDQLALLKEL
TEGLIEDDKVLLQQLISTISNWKNDLKTPSQAAASAIGERDRIFAHCYGLYDAHLKACNV
LDFDDLILLPTLLLQRNEEVRKRWQNKIRYLLVDEYQDTNTSQYELVKLLVGSRARFTVV
GDDDQSIYSWRGARPQNLVLLSQDFPALKVIKLEQNYRSSGRILKAANILIANNPHVFEK
RLFSELGYGAELKVLSANNEEHEAERVTGELIAHHFVNKTQYKDYAILYRGNHQSRVFEK
FLMQNRIPYKISGGTSFFSRPEIKDLLAYLRVLTNPDDDSAFLRIVNTPKREIGPATLKK
LGEWAMTRNKSMFTASFDMGLSQTLSGRGYEALTRFTHWLAEIQRLAEREPIAAVRDLIH
GMDYESWLYETSPSPKAAEMRMKNVNQLFSWMTEMLEGSELDEPMTLTQVVTRFTLRDMM
ERGESEEELDQVQLMTLHASKGLEFPYVYMVGMEEGFLPHQSSIDEDNIDEERRLAYVGI
TRAQKELTFTLCKERRQYGELVRPEPSRFLLELPQDDLIWEQERKVVSAEERMQKGQSHL
ANLKAMMAAKRGK
References
External Links:
ResourceLink
Uniprot ID:P09980
Uniprot Name:REP_ECOLI
GenBank Gene ID:M87049
Genebank Protein ID:148182
PDB ID:1UAA
CCDB:REP_ECOLI
General Reference:
  • Bialkowska-Hobrzanska, H., Gilchrist, C. A., Denhardt, D. T. (1985). "Escherichia coli rep gene: identification of the promoter and N terminus of the rep protein." J Bacteriol 164:1004-1010. Pubmed: 2999067
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
  • Gilchrist, C. A., Denhardt, D. T. (1987). "Escherichia coli rep gene: sequence of the gene, the encoded helicase, and its homology with uvrD." Nucleic Acids Res 15:465-475. Pubmed: 3029683
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Korolev, S., Hsieh, J., Gauss, G. H., Lohman, T. M., Waksman, G. (1997). "Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP." Cell 90:635-647. Pubmed: 9288744
  • Riley, M., Abe, T., Arnaud, M. B., Berlyn, M. K., Blattner, F. R., Chaudhuri, R. R., Glasner, J. D., Horiuchi, T., Keseler, I. M., Kosuge, T., Mori, H., Perna, N. T., Plunkett, G. 3rd, Rudd, K. E., Serres, M. H., Thomas, G. H., Thomson, N. R., Wishart, D., Wanner, B. L. (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34:1-9. Pubmed: 16397293