ID A0A1E7TUG3_9BURK Unreviewed; 329 AA. AC A0A1E7TUG3; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 02-OCT-2024, entry version 38. DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000256|ARBA:ARBA00015972, 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|ARBA:ARBA00012418, ECO:0000256|HAMAP-Rule:MF_00059}; DE AltName: Full=RNA polymerase subunit alpha {ECO:0000256|ARBA:ARBA00033070, ECO:0000256|HAMAP-Rule:MF_00059}; DE AltName: Full=Transcriptase subunit alpha {ECO:0000256|ARBA:ARBA00032524, ECO:0000256|HAMAP-Rule:MF_00059}; GN Name=rpoA {ECO:0000256|HAMAP-Rule:MF_00059}; GN ORFNames=CKY39_31435 {ECO:0000313|EMBL:ATA57236.1}, J2W26_004379 GN {ECO:0000313|EMBL:MDP9880052.1}; OS Variovorax boronicumulans. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=436515 {ECO:0000313|EMBL:ATA57236.1, ECO:0000313|Proteomes:UP000217154}; RN [1] {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. RN [2] {ECO:0000313|EMBL:MDP9880052.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DS2796 {ECO:0000313|EMBL:MDP9880052.1}; RA Schachtman D.; RT "Sorghum-associated microbial communities from plants grown in Nebraska, RT USA."; RL Submitted (JUL-2023) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC {ECO:0000256|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:0000256|ARBA:ARBA00024550, CC 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 associated CC with the core the holoenzyme is formed, which can initiate CC transcription. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00059}. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC {ECO:0000256|ARBA:ARBA00007123, 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; JAUSRS010000007; MDP9880052.1; -; Genomic_DNA. DR RefSeq; WP_056576973.1; NZ_MRCN01000023.1. DR AlphaFoldDB; A0A1E7TUG3; -. DR STRING; 436515.GCA_001752345_06095; -. DR GeneID; 82272234; -. DR KEGG; vbo:CKY39_31435; -. DR OrthoDB; 9805706at2; -. DR Proteomes; UP000217154; Chromosome. DR Proteomes; UP001233434; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. 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 {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_00059}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_00059}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_00059}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00059}. FT DOMAIN 20..230 FT /note="DNA-directed RNA polymerase RpoA/D/Rpb3-type" FT /evidence="ECO:0000259|SMART:SM00662" FT REGION 1..231 FT /note="Alpha N-terminal domain (alpha-NTD)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059" FT REGION 249..329 FT /note="Alpha C-terminal domain (alpha-CTD)" FT /evidence="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 //