DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription. 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. Although RpoA was believed to be phosphorylated by StkP in vivo in a first study (PubMed:15720398), the same authors later showed that this protein is indeed not phosphorylated (PubMed:20453092). Belongs to the RNA polymerase alpha chain family.