Identification |
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Name: | ATP-dependent RNA helicase srmB |
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Synonyms: | Not Available |
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Gene Name: | srmB |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Replication, recombination and repair |
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Specific Function: | RNA-dependent ATPase activity. Acts in 50S ribosomal subunit biogenesis at low temperatures, acting before deaD/csdA. Suppressor of a mutant defective in 50S ribosomal subunit assembly. Probably interacts with 23S ribosomal RNA |
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Cellular Location: | Cytoplasmic |
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SMPDB Pathways: | Not Available |
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KEGG Pathways: | Not Available |
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Complex Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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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 |
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Gene Properties |
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Blattner: | Not Available |
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Gene Orientation | Not Available |
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Centisome Percentage: | Not Available |
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Left Sequence End | Not Available |
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Right Sequence End | Not Available |
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Gene Sequence: | >1335 bp
ATGACTGTAACGACTTTTTCCGAACTTGAACTCGACGAAAGCCTGCTGGAAGCCCTCCAG
GATAAAGGTTTCACTCGCCCGACCGCCATTCAGGCTGCCGCCATTCCGCCTGCGCTCGAT
GGCCGTGATGTACTCGGTTCTGCGCCGACAGGCACCGGTAAAACGGCGGCGTATCTGCTG
CCAGCGTTGCAGCACCTGCTCGATTTCCCGCGTAAGAAATCCGGTCCGCCGCGTATTTTG
ATCCTCACCCCAACTCGCGAGCTGGCGATGCAGGTGTCCGATCATGCCCGCGAACTGGCG
AAACATACGCATCTGGATATCGCCACCATCACCGGCGGCGTAGCCTATATGAACCACGCG
GAAGTGTTCAGCGAAAATCAGGACATCGTGGTCGCCACGACCGGACGTCTGCTGCAATAC
ATAAAAGAAGAGAACTTCGATTGCCGCGCGGTTGAAACGCTGATCCTCGACGAAGCAGAC
CGTATGCTGGATATGGGCTTCGCTCAGGATATCGAACATATTGCTGGCGAAACGCGCTGG
CGTAAACAGACCCTGCTCTTTTCGGCAACGCTGGAAGGCGATGCGATTCAGGACTTTGCC
GAGCGTCTGCTGGAAGATCCGGTGGAAGTTTCTGCCAATCCCTCCACCCGTGAGCGCAAA
AAAATTCATCAGTGGTATTACCGCGCCGATGATCTTGAGCATAAAACCGCGTTGCTGGTG
CATCTGTTAAAACAGCCGGAAGCGACCCGCTCAATTGTGTTTGTGCGTAAGCGTGAGCGT
GTGCATGAGCTGGCAAACTGGCTGCGCGAAGCGGGCATCAACAACTGCTATCTCGAAGGT
GAGATGGTACAGGGCAAGCGTAACGAAGCGATCAAGCGTTTGACCGAAGGTCGCGTAAAC
GTACTGGTCGCAACCGATGTTGCCGCGCGCGGTATCGACATTCCTGACGTCAGCCACGTC
TTTAACTTCGATATGCCGCGCAGTGGCGATACTTATTTGCACCGTATCGGACGTACCGCG
CGCGCCGGTCGTAAAGGCACCGCAATTTCGCTGGTGGAAGCCCATGACCATCTGCTGCTG
GGTAAAGTAGGCCGCTATATTGAAGAGCCAATTAAAGCTCGCGTTATTGATGAGTTACGC
CCGAAAACGCGTGCGCCAAGCGAAAAGCAGACCGGCAAGCCATCGAAGAAAGTACTGGCT
AAACGTGCTGAGAAGAAAAAAGCTAAAGAGAAAGAGAAGCCGCGGGTGAAAAAACGCCAT
CGCGACACCAAAAATATTGGTAAGCGCCGTAAACCAAGCGGAACGGGCGTGCCACCGCAA
ACGACAGAAGAGTAA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 444 |
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Protein Molecular Weight: | 49914 |
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Protein Theoretical pI: | 10 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >ATP-dependent RNA helicase srmB
MTVTTFSELELDESLLEALQDKGFTRPTAIQAAAIPPALDGRDVLGSAPTGTGKTAAYLL
PALQHLLDFPRKKSGPPRILILTPTRELAMQVSDHARELAKHTHLDIATITGGVAYMNHA
EVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIEHIAGETRW
RKQTLLFSATLEGDAIQDFAERLLEDPVEVSANPSTRERKKIHQWYYRADDLEHKTALLV
HLLKQPEATRSIVFVRKRERVHELANWLREAGINNCYLEGEMVQGKRNEAIKRLTEGRVN
VLVATDVAARGIDIPDVSHVFNFDMPRSGDTYLHRIGRTARAGRKGTAISLVEAHDHLLL
GKVGRYIEEPIKARVIDELRPKTRAPSEKQTGKPSKKVLAKRAEKKKAKEKEKPRVKKRH
RDTKNIGKRRKPSGTGVPPQTTEE |
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References |
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External Links: | |
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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
- Charollais, J., Dreyfus, M., Iost, I. (2004). "CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in the biogenesis of 50S ribosomal subunit." Nucleic Acids Res 32:2751-2759. Pubmed: 15148362
- 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
- Nishi, K., Morel-Deville, F., Hershey, J. W., Leighton, T., Schnier, J. (1988). "An eIF-4A-like protein is a suppressor of an Escherichia coli mutant defective in 50S ribosomal subunit assembly." Nature 336:496-498. Pubmed: 2461520
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