ID RPOA_THETH Reviewed; 315 AA. AC Q9Z9H6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 134. DE RecName: Full=DNA-directed RNA polymerase subunit alpha; DE Short=RNAP subunit alpha; DE EC=2.7.7.6; DE AltName: Full=RNA polymerase subunit alpha; DE AltName: Full=Transcriptase subunit alpha; GN Name=rpoA; OS Thermus thermophilus. OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=274; RN [1] RP STRUCTURE BY NMR OF 247-315. RX PubMed=10821859; DOI=10.1074/jbc.275.21.16057; RA Wada T., Yamazaki T., Kyogoku Y.; RT "The structure and the characteristic DNA binding property of the C- RT terminal domain of the RNA polymerase alpha subunit from Thermus RT thermophilus."; RL J. Biol. Chem. 275:16057-16063(2000). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=12000971; DOI=10.1038/nature752; RA Vassylyev D.G., Sekine S., Laptenko O., Lee J., Vassylyeva M.N., RA Borukhov S., Yokoyama S.; RT "Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A RT resolution."; RL Nature 417:712-719(2002). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. 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; 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. 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:0000250}. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC {ECO:0000305}. CC -!- CAUTION: The sequence shown here has been extracted from PDB entry CC 1IW7. {ECO:0000305}. 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 RefSeq; WP_011173698.1; NZ_DFSU01000131.1. DR PDB; 1DOQ; NMR; -; A=247-315. DR PDB; 1IW7; X-ray; 2.60 A; A/B/K/L=1-315. DR PDB; 1SMY; X-ray; 2.70 A; A/B/K/L=1-315. DR PDB; 2BE5; X-ray; 2.40 A; A/B/K/L=1-315. DR PDB; 2PPB; X-ray; 3.00 A; A/B/K/L=1-315. DR PDB; 3EQL; X-ray; 2.70 A; A/B/K/L=1-315. DR PDB; 4Q4Z; X-ray; 2.90 A; A/B=1-315. DR PDB; 4Q5S; X-ray; 3.00 A; A/B=1-315. DR PDBsum; 1DOQ; -. DR PDBsum; 1IW7; -. DR PDBsum; 1SMY; -. DR PDBsum; 2BE5; -. DR PDBsum; 2PPB; -. DR PDBsum; 3EQL; -. DR PDBsum; 4Q4Z; -. DR PDBsum; 4Q5S; -. DR AlphaFoldDB; Q9Z9H6; -. DR BMRB; Q9Z9H6; -. DR SMR; Q9Z9H6; -. DR DIP; DIP-60256N; -. DR IntAct; Q9Z9H6; 3. DR DrugBank; DB08226; Myxopyronin B. DR GeneID; 3169128; -. DR OMA; PIKNVKY; -. DR EvolutionaryTrace; Q9Z9H6; -. 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 1: Evidence at protein level; KW 3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase; KW Transcription; Transferase. FT CHAIN 1..315 FT /note="DNA-directed RNA polymerase subunit alpha" FT /id="PRO_0000175409" FT REGION 1..229 FT /note="Alpha N-terminal domain (alpha-NTD)" FT REGION 247..315 FT /note="Alpha C-terminal domain (alpha-CTD)" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 10..16 FT /evidence="ECO:0007829|PDB:1IW7" FT TURN 17..19 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 20..28 FT /evidence="ECO:0007829|PDB:1IW7" FT HELIX 32..46 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 48..60 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 71..74 FT /evidence="ECO:0007829|PDB:1IW7" FT HELIX 75..83 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 95..106 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:1IW7" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 128..132 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 137..151 FT /evidence="ECO:0007829|PDB:1IW7" FT HELIX 153..156 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 160..163 FT /evidence="ECO:0007829|PDB:4Q5S" FT STRAND 173..181 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 193..201 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:1IW7" FT HELIX 207..223 FT /evidence="ECO:0007829|PDB:1IW7" FT HELIX 256..259 FT /evidence="ECO:0007829|PDB:1DOQ" FT HELIX 263..271 FT /evidence="ECO:0007829|PDB:1DOQ" FT HELIX 277..282 FT /evidence="ECO:0007829|PDB:1DOQ" FT HELIX 285..288 FT /evidence="ECO:0007829|PDB:1DOQ" FT HELIX 296..309 FT /evidence="ECO:0007829|PDB:1DOQ" SQ SEQUENCE 315 AA; 35013 MW; F79D93B57526A1CB CRC64; MLDSKLKAPV FTVRTQGREY GEFVLEPLER GFGVTLGNPL RRILLSSIPG TAVTSVYIED VLHEFSTIPG VKEDVVEIIL NLKELVVRFL NPSLQTVTLL LKAEGPKEVK ARDFLPVADV EIMNPDLHIA TLEEGGRLNM EVRVDRGVGY VPAEKHGIKD RINAIPVDAV FSPVRRVAFQ VEDTRLGQRT DLDKLTLRIW TDGSVTPLEA LNQAVEILRE HLTYFSNPQA AAVAAPEEAK EPEAPPEQEE ELDLPLEELG LSTRVLHSLK EEGIESVRAL LALNLKDLKN IPGIGERSLE EIKEALEKKG FTLKE //