ID RPOA_HELPY Reviewed; 344 AA. AC P56001; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 136. DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE Short=RNAP subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059}; DE AltName: Full=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE AltName: Full=Transcriptase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; GN Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059}; GN OrderedLocusNames=HP_1293; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC {ECO:0000255|HAMAP-Rule:MF_00059}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00059}; CC -!- SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1 CC beta, 1 beta' and 1 omega subunit. When a sigma factor is associated CC with the core the holoenzyme is formed, which can initiate CC transcription. {ECO:0000255|HAMAP-Rule:MF_00059}. CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal CC transcription, whereas the C-terminal domain is involved in interaction CC with transcriptional regulators and with upstream promoter elements. CC {ECO:0000255|HAMAP-Rule:MF_00059}. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC {ECO:0000255|HAMAP-Rule:MF_00059}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000511; AAD08336.1; -; Genomic_DNA. DR PIR; E64681; E64681. DR RefSeq; NP_208085.1; NC_000915.1. DR RefSeq; WP_000864547.1; NC_018939.1. DR AlphaFoldDB; P56001; -. DR BMRB; P56001; -. DR SMR; P56001; -. DR DIP; DIP-3396N; -. DR IntAct; P56001; 2. DR MINT; P56001; -. DR STRING; 85962.HP_1293; -. DR PaxDb; 85962-C694_06680; -. DR EnsemblBacteria; AAD08336; AAD08336; HP_1293. DR KEGG; hpy:HP_1293; -. DR PATRIC; fig|85962.47.peg.1387; -. DR eggNOG; COG0202; Bacteria. DR InParanoid; P56001; -. DR OrthoDB; 9805706at2; -. DR PhylomeDB; P56001; -. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR CDD; cd06928; RNAP_alpha_NTD; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 2.170.120.12; DNA-directed RNA polymerase, insert domain; 1. DR Gene3D; 3.30.1360.10; RNA polymerase, RBP11-like subunit; 1. DR HAMAP; MF_00059; RNApol_bact_RpoA; 1. DR InterPro; IPR011262; DNA-dir_RNA_pol_insert. DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3. DR InterPro; IPR011773; DNA-dir_RpoA. DR InterPro; IPR036603; RBP11-like. DR InterPro; IPR011260; RNAP_asu_C. DR InterPro; IPR036643; RNApol_insert_sf. DR NCBIfam; TIGR02027; rpoA; 1. DR Pfam; PF01000; RNA_pol_A_bac; 1. DR Pfam; PF03118; RNA_pol_A_CTD; 1. DR Pfam; PF01193; RNA_pol_L; 1. DR SMART; SM00662; RPOLD; 1. DR SUPFAM; SSF47789; C-terminal domain of RNA polymerase alpha subunit; 1. DR SUPFAM; SSF56553; Insert subdomain of RNA polymerase alpha subunit; 1. DR SUPFAM; SSF55257; RBP11-like subunits of RNA polymerase; 1. PE 3: Inferred from homology; KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome; KW Transcription; Transferase. FT CHAIN 1..344 FT /note="DNA-directed RNA polymerase subunit alpha" FT /id="PRO_0000175316" FT REGION 1..238 FT /note="Alpha N-terminal domain (alpha-NTD)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059" FT REGION 254..344 FT /note="Alpha C-terminal domain (alpha-CTD)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059" SQ SEQUENCE 344 AA; 38499 MW; 0F812B0020DF7414 CRC64; MKVIKTAPLI PSEIKVLEKE GNRVKISLAP FEFGYAVTLA HPIRRLLLLS SVGYAPVGLK IEGVHHEFDS LRGVTEDVSL FIMNLKNIRF IAKALVGQDS SLENQSVVVD YSFKGPMELR ARDLNSEQIE IVNPEMPLAT INEDAQLNFS LIIYKGMGYV PSENTRELMP EGYMPLDGSF TPIKKVVYEI ENVLVEGDPN YEKIIFDIET DGQIDPYKAF LSAVKVMSKQ LGVFGERPIA NTEYSGDYAQ RDDAKDLSAK IESMNLSARC FNCLDKIGIK YVGELVLMSE EELKGVKNMG KKSYDEIAEK LNDLGYPVGT ELSPEQRESL KKRLEKLEDK GGND //