ID A0A1E7TUG3_9BURK Unreviewed; 329 AA. AC A0A1E7TUG3; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 31-JAN-2018, entry version 10. DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059}; DE Short=RNAP subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00059}; DE AltName: Full=RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059}; DE AltName: Full=Transcriptase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059}; GN Name=rpoA {ECO:0000256|HAMAP-Rule:MF_00059}; GN ORFNames=AO062_27730 {ECO:0000313|EMBL:OEZ27482.1}, CKY39_31435 GN {ECO:0000313|EMBL:ATA57236.1}; OS Variovorax boronicumulans. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=436515 {ECO:0000313|EMBL:OEZ27482.1, ECO:0000313|Proteomes:UP000175920}; RN [1] {ECO:0000313|Proteomes:UP000175920} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PHE5-4 {ECO:0000313|Proteomes:UP000175920}; RA Tabata M.; RT "Whole genome sequence of Cupriavidus necator strain PHE3-6."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:OEZ27482.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PHE5-4 {ECO:0000313|EMBL:OEZ27482.1}; RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E., RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M., RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ATA57236.1, ECO:0000313|Proteomes:UP000217154} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J1 {ECO:0000313|EMBL:ATA57236.1, RC ECO:0000313|Proteomes:UP000217154}; RA Sun S.; RT "The diverse metabolic capabilities of V. boronicumulans make it an RT excellent choice for continued studies on novel biodegradation."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {ECO:0000256|HAMAP-Rule:MF_00059}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000256|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 CC associated with the core the holoenzyme is formed, which can CC initiate transcription. {ECO:0000256|HAMAP-Rule:MF_00059}. CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and CC basal transcription, whereas the C-terminal domain is involved in CC interaction with transcriptional regulators and with upstream CC promoter elements. {ECO:0000256|HAMAP-Rule:MF_00059}. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC {ECO:0000256|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; CP023284; ATA57236.1; -; Genomic_DNA. DR EMBL; LKDZ01000048; OEZ27482.1; -; Genomic_DNA. DR RefSeq; WP_056576973.1; NZ_MRCN01000023.1. DR EnsemblBacteria; OEZ27482; OEZ27482; AO062_27730. DR KEGG; vbo:CKY39_31435; -. DR KO; K03040; -. DR Proteomes; UP000175920; Unassembled WGS sequence. DR Proteomes; UP000217154; Chromosome. 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:transcription, DNA-templated; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.1360.10; -; 2. 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 Pfam; PF01000; RNA_pol_A_bac; 1. DR Pfam; PF03118; RNA_pol_A_CTD; 1. DR Pfam; PF01193; RNA_pol_L; 1. DR ProDom; PD001179; RNAP_asu_C; 1. DR SMART; SM00662; RPOLD; 1. DR SUPFAM; SSF55257; SSF55257; 2. DR SUPFAM; SSF56553; SSF56553; 1. DR TIGRFAMs; TIGR02027; rpoA; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000175920, KW ECO:0000313|Proteomes:UP000217154}; KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00059, KW ECO:0000313|EMBL:OEZ27482.1}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00059, KW ECO:0000313|EMBL:OEZ27482.1}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00059}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00059, KW ECO:0000313|EMBL:OEZ27482.1}. FT DOMAIN 20 230 RPOLD. {ECO:0000259|SMART:SM00662}. FT REGION 1 231 Alpha N-terminal domain (alpha-NTD). FT {ECO:0000256|HAMAP-Rule:MF_00059}. FT REGION 249 329 Alpha C-terminal domain (alpha-CTD). FT {ECO:0000256|HAMAP-Rule:MF_00059}. SQ SEQUENCE 329 AA; 36168 MW; 160A4A3E1695E6C2 CRC64; MQTTLLKPKT IQVEQLAANK AKVTLEPFER GYGHTLGNAL RRVLLSSMVG YSATEVTIAG VLHEYSSIDG VQEDVVNILL NLKGVVFKLH NRDEVTLSLR KDGEGPVLAS DIQTPHDVEI INPDHVIAHL SQGGKLDMQI KVEKGRGYVP GTMRRYADEP TKSIGRIVLD ASFSPVKRVS YTVESARVEQ RTDLDKLLVE IETNGAISAE DAVRASAKIL VEQLAVFAQL EGGELAAFDA PAPRSAQQFD PILLRPVDEL ELTVRSANCL KAENIYYIGD LIQRTENELL KTPNLGRKSL NEIKEVLASR GLTLGMKLES WPPAGLDKR //