RNA polymerase sigma factor SigA

Details

Name
RNA polymerase sigma factor SigA
Synonyms
  • RpoD
Gene Name
sigA
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Amino acid sequence
>lcl|BSEQ0012357|RNA polymerase sigma factor SigA
MKKSKRKNAQAQEAQETEVLVQEEAEELPEFPEGEPDPDLEDPDLTLEDDLLDLPEEGEG
LDLEEEEEDLPIPKISTSDPVRQYLHEIGQVPLLTLEEEVELARKVEEGMEAIKKLSEIT
GLDPDLIREVVRAKILGSARVRHIPGLKETLDPKTVEEIDQKLKSLPKEHKRYLHIAREG
EAARQHLIEANLRLVVSIAKKYTGRGLSFLDLIQEGNQGLIRAVEKFEYKRRFKFSTYAT
WWIRQAINRAIADQARTIRIPVHMVETINKLSRTARQLQQELGREPTYEEIAEAMGPGWD
AKRVEETLKIAQEPVSLETPIGDEKDSFYGDFIPDEHLPSPVDAATQSLLSEELEKALSK
LSEREAMVLKLRKGLIDGREHTLEEVGAFFGVTRERIRQIENKALRKLKYHESRTRKLRD
FLD
Number of residues
423
Molecular Weight
48523.59
Theoretical pI
4.77
GO Classification
Functions
DNA binding / metal ion binding / sigma factor activity / transcription factor activity, sequence-specific DNA binding
Processes
transcription initiation from bacterial-type RNA polymerase promoter
Components
cytoplasm
General Function
Transcription factor activity, sequence-specific dna binding
Specific Function
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0012358|RNA polymerase sigma factor SigA (sigA)
TTGAAGAAGAGCAAGCGCAAGAACGCCCAGGCCCAGGAGGCCCAGGAGACCGAGGTCCTG
GTCCAGGAGGAGGCGGAGGAACTCCCCGAGTTCCCCGAGGGGGAGCCCGACCCCGACCTC
GAGGACCCGGACCTCACCCTGGAGGACGACCTCCTGGACCTGCCCGAGGAGGGCGAGGGG
CTGGACCTGGAGGAGGAGGAAGAAGACCTCCCCATCCCCAAGATCTCCACCTCCGACCCC
GTGCGCCAGTACCTGCACGAGATCGGCCAGGTCCCCCTCCTCACCCTGGAGGAGGAGGTG
GAGCTCGCCCGGAAGGTGGAGGAGGGGATGGAGGCCATCAAGAAGCTCTCCGAGATCACC
GGCCTTGACCCCGACCTCATCCGGGAGGTGGTCCGGGCCAAGATTCTGGGCTCGGCCCGG
GTGCGGCACATCCCCGGCCTCAAGGAGACCCTGGACCCCAAGACCGTGGAGGAGATTGAC
CAGAAGCTCAAAAGCCTCCCCAAGGAGCACAAGCGCTACCTCCACATCGCCCGGGAAGGG
GAGGCGGCCCGGCAGCACCTCATTGAGGCCAACCTCCGGCTCGTGGTCTCCATCGCCAAG
AAGTACACGGGGCGGGGCCTCTCCTTCCTGGACCTCATCCAGGAGGGAAACCAGGGCCTG
ATCCGGGCGGTGGAGAAGTTTGAGTACAAGCGGCGCTTCAAGTTCTCCACCTACGCCACC
TGGTGGATCCGGCAGGCCATCAACCGGGCCATCGCCGACCAGGCCCGCACCATCCGCATC
CCGGTCCACATGGTGGAGACCATCAACAAGCTCTCCCGCACCGCAAGGCAGCTGCAGCAG
GAGCTCGGCCGGGAACCCACCTACGAGGAGATCGCCGAGGCCATGGGGCCGGGCTGGGAC
GCCAAGCGGGTGGAGGAAACCCTCAAGATCGCCCAGGAGCCCGTCTCCCTGGAGACCCCC
ATCGGCGACGAGAAGGACAGCTTCTACGGGGACTTCATCCCCGACGAGCACCTCCCCTCC
CCGGTGGACGCCGCCACCCAGAGCCTCCTCTCCGAGGAGCTGGAGAAGGCCCTGTCCAAG
CTCTCCGAGCGCGAGGCCATGGTCCTGAAGCTCCGGAAAGGGCTCATTGACGGGCGGGAG
CACACCCTGGAGGAGGTGGGGGCCTTCTTCGGCGTCACCCGGGAAAGGATCCGGCAGATT
GAGAACAAGGCCCTCCGCAAGCTCAAGTACCACGAGTCCCGCACGCGGAAGCTCAGGGAC
TTCCTGGACTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ5SKW1
UniProtKB Entry NameQ5SKW1_THET8
GenBank Gene IDAP008226
General References
  1. Artsimovitch I, Vassylyeva MN, Svetlov D, Svetlov V, Perederina A, Igarashi N, Matsugaki N, Wakatsuki S, Tahirov TH, Vassylyev DG: Allosteric modulation of the RNA polymerase catalytic reaction is an essential component of transcription control by rifamycins. Cell. 2005 Aug 12;122(3):351-63. [PubMed:16096056]
  2. Tuske S, Sarafianos SG, Wang X, Hudson B, Sineva E, Mukhopadhyay J, Birktoft JJ, Leroy O, Ismail S, Clark AD Jr, Dharia C, Napoli A, Laptenko O, Lee J, Borukhov S, Ebright RH, Arnold E: Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation. Cell. 2005 Aug 26;122(4):541-52. [PubMed:16122422]
  3. Temiakov D, Zenkin N, Vassylyeva MN, Perederina A, Tahirov TH, Kashkina E, Savkina M, Zorov S, Nikiforov V, Igarashi N, Matsugaki N, Wakatsuki S, Severinov K, Vassylyev DG: Structural basis of transcription inhibition by antibiotic streptolydigin. Mol Cell. 2005 Sep 2;19(5):655-66. [PubMed:16167380]
  4. Vassylyev DG, Svetlov V, Vassylyeva MN, Perederina A, Igarashi N, Matsugaki N, Wakatsuki S, Artsimovitch I: Structural basis for transcription inhibition by tagetitoxin. Nat Struct Mol Biol. 2005 Dec;12(12):1086-93. Epub 2005 Nov 6. [PubMed:16273103]
  5. Mukhopadhyay J, Das K, Ismail S, Koppstein D, Jang M, Hudson B, Sarafianos S, Tuske S, Patel J, Jansen R, Irschik H, Arnold E, Ebright RH: The RNA polymerase "switch region" is a target for inhibitors. Cell. 2008 Oct 17;135(2):295-307. doi: 10.1016/j.cell.2008.09.033. [PubMed:18957204]
  6. Belogurov GA, Vassylyeva MN, Sevostyanova A, Appleman JR, Xiang AX, Lira R, Webber SE, Klyuyev S, Nudler E, Artsimovitch I, Vassylyev DG: Transcription inactivation through local refolding of the RNA polymerase structure. Nature. 2009 Jan 15;457(7227):332-5. doi: 10.1038/nature07510. Epub 2008 Oct 22. [PubMed:18946472]
  7. Zhang Y, Feng Y, Chatterjee S, Tuske S, Ho MX, Arnold E, Ebright RH: Structural basis of transcription initiation. Science. 2012 Nov 23;338(6110):1076-80. doi: 10.1126/science.1227786. Epub 2012 Oct 18. [PubMed:23086998]
  8. Zhang Y, Degen D, Ho MX, Sineva E, Ebright KY, Ebright YW, Mekler V, Vahedian-Movahed H, Feng Y, Yin R, Tuske S, Irschik H, Jansen R, Maffioli S, Donadio S, Arnold E, Ebright RH: GE23077 binds to the RNA polymerase 'i' and 'i+1' sites and prevents the binding of initiating nucleotides. Elife. 2014 Apr 22;3:e02450. doi: 10.7554/eLife.02450. [PubMed:24755292]
  9. Tagami S, Sekine S, Minakhin L, Esyunina D, Akasaka R, Shirouzu M, Kulbachinskiy A, Severinov K, Yokoyama S: Structural basis for promoter specificity switching of RNA polymerase by a phage factor. Genes Dev. 2014 Mar 1;28(5):521-31. doi: 10.1101/gad.233916.113. [PubMed:24589779]
  10. Basu RS, Warner BA, Molodtsov V, Pupov D, Esyunina D, Fernandez-Tornero C, Kulbachinskiy A, Murakami KS: Structural basis of transcription initiation by bacterial RNA polymerase holoenzyme. J Biol Chem. 2014 Aug 29;289(35):24549-59. doi: 10.1074/jbc.M114.584037. Epub 2014 Jun 27. [PubMed:24973216]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB08226Myxopyronin BexperimentalunknownDetails
DB08266Methyl [(1E,5R)-5-{3-[(2E,4E)-2,5-dimethyl-2,4-octadienoyl]-2,4-dioxo-3,4-dihydro-2H-pyran-6-yl}hexylidene]carbamateexperimentalunknownDetails