ECMDB: ATP-dependent RNA helicase rhlE (P25888)

Identification

Name:

ATP-dependent RNA helicase rhlE

Synonyms:

Not Available

Gene Name:

rhlE

Enzyme Class:

3.6.4.13

Biological Properties

General Function:

Replication, recombination and repair

Specific Function:

Acts as an ATP-dependent RNA helicase, able to unwind ds-RNA

Cellular Location:

Cytoplasmic

SMPDB Pathways:

Not Available

KEGG Pathways:

RNA degradation eco03018

Metabolites:

ECMDB ID	Name	View
ECMDB00538	Adenosine triphosphate	MetaboCard
ECMDB01341	ADP	MetaboCard
ECMDB21380	Inorganic phosphate	MetaboCard
ECMDB00494	Water	MetaboCard

GO Classification:

Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
ATP-dependent helicase activity
ATPase activity
ATPase activity, coupled
binding
catalytic 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

Gene Properties

Blattner:

Not Available

Gene Orientation

Not Available

Centisome Percentage:

Not Available

Left Sequence End

Not Available

Right Sequence End

Not Available

Gene Sequence:

>1365 bp
ATGTCTTTCGATTCTTTGGGTTTAAGCCCTGATATCCTGCGCGCCGTTGCCGAGCAGGGT
TACCGTGAACCCACCCCTATTCAGCAGCAGGCGATCCCTGCGGTGCTGGAAGGCCGCGAC
CTGATGGCTAGCGCCCAGACCGGCACCGGCAAAACAGCGGGCTTTACGCTGCCGCTGTTG
CAACACCTGATCACTCGCCAGCCGCACGCCAAAGGGCGTCGTCCGGTACGTGCGCTCATT
CTTACCCCGACCCGTGAACTGGCGGCGCAGATTGGCGAAAACGTCCGTGATTACAGCAAA
TACCTGAACATTCGTTCGCTGGTGGTGTTTGGTGGTGTGAGTATTAACCCGCAGATGATG
AAACTGCGTGGCGGCGTTGATGTGCTGGTGGCAACCCCGGGACGTTTGCTGGACCTGGAA
CATCAGAATGCAGTGAAGCTGGATCAGGTTGAAATCCTCGTCCTCGATGAAGCTGACCGC
ATGCTCGACATGGGCTTTATCCACGATATCCGTCGCGTGTTAACAAAACTACCTGCGAAG
CGCCAGAACCTGTTATTCTCCGCGACCTTCTCTGACGATATTAAAGCCCTGGCGGAAAAA
CTGTTGCACAACCCGCTGGAAATCGAAGTGGCACGCCGCAATACCGCGTCTGATCAGGTG
ACCCAGCACGTTCACTTTGTCGATAAGAAACGCAAACGCGAATTGCTGTCGCACATGATT
GGGAAAGGGAACTGGCAGCAGGTGCTGGTGTTTACCCGTACCAAACACGGCGCTAACCAT
CTGGCTGAACAGCTCAATAAAGATGGCATCCGTAGTGCGGCGATCCACGGCAATAAATCG
CAAGGTGCGCGTACTCGTGCGCTGGCTGATTTTAAATCGGGCGATATTCGTGTACTGGTG
GCAACTGACATCGCTGCGCGCGGCCTGGATATTGAAGAGCTGCCGCACGTCGTCAACTAT
GAACTGCCAAACGTACCTGAAGATTATGTCCACCGTATCGGGCGTACCGGTCGTGCGGCT
GCTACCGGTGAAGCGTTGTCGCTGGTGTGTGTTGATGAACACAAACTGCTGCGTGATATC
GAAAAACTGCTGAAAAAAGAGATCCCGCGCATTGCGATTCCGGGCTATGAGCCGGACCCG
TCAATCAAAGCCGAACCGATCCAGAACGGTCGCCAGCAACGTGGCGGCGGCGGTCGTGGG
CAAGGTGGTGGTCGCGGTCAACAGCAACCACGCCGTGGGGAAGGTGGCGCAAAATCTGCA
AGCGCGAAACCTGCAGAAAAACCGTCTCGCCGCCTCGGCGATGCCAAACCGGCAGGCGAA
CAACAACGTCGCCGCCGTCCGCGTAAACCTGCCGCTGCGCAGTAA

Protein Properties

Pfam Domain Function:

Helicase_C (PF00271 )
DEAD (PF00270 )

Protein Residues:

454

Protein Molecular Weight:

49989

Protein Theoretical pI:

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>ATP-dependent RNA helicase rhlE
MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLL
QHLITRQPHAKGRRPVRALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMM
KLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLTKLPAK
RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASDQVTQHVHFVDKKRKRELLSHMI
GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLV
ATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDI
EKLLKKEIPRIAIPGYEPDPSIKAEPIQNGRQQRGGGGRGQGGGRGQQQPRRGEGGAKSA
SAKPAEKPSRRLGDAKPAGEQQRRRRPRKPAAAQ

References

External Links:

Resource	Link
Uniprot ID:	P25888
Uniprot Name:	RHLE_ECOLI
GenBank Gene ID:	L02123
Genebank Protein ID:	560801
CCDB:	RHLE_ECOLI

General Reference:

Bizebard, T., Ferlenghi, I., Iost, I., Dreyfus, M. (2004). "Studies on three E. coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases." Biochemistry 43:7857-7866. Pubmed: 15196029
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
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
Kalman, M., Murphy, H., Cashel, M. (1991). "rhlB, a new Escherichia coli K-12 gene with an RNA helicase-like protein sequence motif, one of at least five such possible genes in a prokaryote." New Biol 3:886-895. Pubmed: 1931833
Ohmori, H. (1994). "Structural analysis of the rhlE gene of Escherichia coli." Jpn J Genet 69:1-12. Pubmed: 8037924
Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
Raynal, L. C., Carpousis, A. J. (1999). "Poly(A) polymerase I of Escherichia coli: characterization of the catalytic domain, an RNA binding site and regions for the interaction with proteins involved in mRNA degradation." Mol Microbiol 32:765-775. Pubmed: 10361280