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        <rdfs:label>B. melitensis 16M rpoA mutant</rdfs:label>
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        <ns3:IAO_0000119>PMID: 14638795</ns3:IAO_0000119>
        <rdfs:comment>Information about the mutated molecule: FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates(Swiss-Prot: Q8G094).  CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)(Swiss-Prot: Q8G094).  SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta&#39; and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription (By similarity)(Swiss-Prot: Q8G094).  DOMAIN: The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements (By similarity)(Swiss-Prot: Q8G094).  SIMILARITY: Belongs to the RNA polymerase alpha chain family(Swiss-Prot: Q8G094).  MUTATION: The rpoA gene codes for the essential alpha-subunit of the RNA polymerase. B. melitensis rpoA mutant was found by signature-tagged mutagenesis from a mouse infection model. This disruption leaves a partially functional protein, impaired for the activation of virB transcription, as demonstrated by the absence of induction of the virB promoter in the Tn5::rpoA background. RpoA is involved in virB regulation in vitro. The mutant (Tn5::rpoA) was more resistant to oxidative stress [Ref6480:Lestrate et al., 2003].</rdfs:comment>
        <ns3:IAO_0000115>A mutant of strain Brucella melitensis bv. 1 str. 16M that lacks an intact gene rpoA.</ns3:IAO_0000115>
        <rdfs:seeAlso>NCBIGene: 1196492</rdfs:seeAlso>
        <ns3:IAO_0000117>YH</ns3:IAO_0000117>
        <rdfs:comment>The gene rpoA from the strain Brucella melitensis bv. 1 str. 16M is a virulence gene.</rdfs:comment>
        <rdfs:seeAlso>UniProtKB accession: Q8YHL6</rdfs:seeAlso>
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