ID RPOZ_THET8 Reviewed; 99 AA. AC Q8RQE7; Q5SI19; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 27-MAR-2024, entry version 133. DE RecName: Full=DNA-directed RNA polymerase subunit omega {ECO:0000255|HAMAP-Rule:MF_00366}; DE Short=RNAP omega subunit {ECO:0000255|HAMAP-Rule:MF_00366}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00366}; DE AltName: Full=RNA polymerase omega subunit {ECO:0000255|HAMAP-Rule:MF_00366}; DE AltName: Full=Transcriptase subunit omega {ECO:0000255|HAMAP-Rule:MF_00366}; GN Name=rpoZ {ECO:0000255|HAMAP-Rule:MF_00366}; GN OrderedLocusNames=TTHA1561; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12198314; DOI=10.1107/s0907444902011770; RA Vassylyeva M.N., Lee J., Sekine S.I., Laptenko O., Kuramitsu S., RA Shibata T., Inoue Y., Borukhov S., Vassylyev D.G., Yokoyama S.; RT "Purification, crystallization and initial crystallographic analysis of RNA RT polymerase holoenzyme from Thermus thermophilus."; RL Acta Crystallogr. D 58:1497-1500(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C- CC terminal regions of the beta' subunit thereby facilitating its CC interaction with the beta and alpha subunits. {ECO:0000255|HAMAP- CC Rule:MF_00366}. 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_00366}; CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' CC and 1 omega subunit. When a sigma factor is associated with the core CC the holoenzyme is formed, which can initiate transcription. CC {ECO:0000255|HAMAP-Rule:MF_00366}. CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family. CC {ECO:0000255|HAMAP-Rule:MF_00366}. 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; AB083791; BAB89402.1; -; Genomic_DNA. DR EMBL; AP008226; BAD71384.1; -; Genomic_DNA. DR RefSeq; WP_008633185.1; NC_006461.1. DR RefSeq; YP_144827.1; NC_006461.1. DR PDB; 1IW7; X-ray; 2.60 A; E/O=1-99. DR PDB; 1SMY; X-ray; 2.70 A; E/O=1-99. DR PDB; 1ZYR; X-ray; 3.00 A; E/O=1-99. DR PDB; 2A68; X-ray; 2.50 A; E/O=1-99. DR PDB; 2A69; X-ray; 2.50 A; E/O=1-99. DR PDB; 2A6E; X-ray; 2.80 A; E/O=1-99. DR PDB; 2A6H; X-ray; 2.40 A; E/O=1-99. DR PDB; 2BE5; X-ray; 2.40 A; E/O=1-99. DR PDB; 2CW0; X-ray; 3.30 A; E/O=1-99. DR PDB; 2O5I; X-ray; 2.50 A; E/O=1-99. DR PDB; 2O5J; X-ray; 3.00 A; E/O=1-99. DR PDB; 2PPB; X-ray; 3.00 A; E/O=1-99. DR PDB; 3AOH; X-ray; 4.10 A; E/J/O=1-99. DR PDB; 3AOI; X-ray; 4.30 A; E/J/O=1-99. DR PDB; 3DXJ; X-ray; 3.00 A; E/O=1-99. DR PDB; 3EQL; X-ray; 2.70 A; E/O=1-99. DR PDB; 3WOD; X-ray; 3.60 A; E=1-99. DR PDB; 4G7H; X-ray; 2.90 A; E/O=1-99. DR PDB; 4G7O; X-ray; 2.99 A; E/O=1-99. DR PDB; 4G7Z; X-ray; 3.82 A; E/O=1-99. DR PDB; 4GZY; X-ray; 3.51 A; E=1-99. DR PDB; 4GZZ; X-ray; 4.29 A; E=1-99. DR PDB; 4MQ9; X-ray; 3.35 A; E=1-99. DR PDB; 4OIN; X-ray; 2.80 A; E=1-99. DR PDB; 4OIO; X-ray; 3.10 A; E=1-99. DR PDB; 4OIP; X-ray; 3.40 A; E=1-99. DR PDB; 4OIQ; X-ray; 3.62 A; E=1-99. DR PDB; 4OIR; X-ray; 3.10 A; E=1-99. DR PDB; 4Q4Z; X-ray; 2.90 A; E=1-99. DR PDB; 4Q5S; X-ray; 3.00 A; E=1-99. DR PDB; 4WQS; X-ray; 4.31 A; E/O=1-99. DR PDB; 4WQT; X-ray; 4.40 A; E/J/O=1-99. DR PDB; 5D4C; X-ray; 3.28 A; E/O=1-99. DR PDB; 5D4D; X-ray; 3.00 A; E/O=1-99. DR PDB; 5D4E; X-ray; 3.08 A; E/O=1-99. DR PDB; 5E17; X-ray; 3.20 A; E=1-99. DR PDB; 5E18; X-ray; 3.30 A; E=1-99. DR PDB; 5I2D; X-ray; 4.41 A; E/P=1-99. DR PDB; 5TMC; X-ray; 2.71 A; E=1-99. DR PDB; 5TMF; X-ray; 3.00 A; E=1-99. DR PDB; 5VO8; X-ray; 3.30 A; E=1-99. DR PDB; 5VOI; X-ray; 2.80 A; E=1-99. DR PDB; 5X21; X-ray; 3.32 A; E=1-99. DR PDB; 5X22; X-ray; 3.35 A; E/O=1-99. DR PDB; 5XJ0; X-ray; 4.00 A; E=1-99. DR PDB; 6ASG; X-ray; 3.80 A; E=1-99. DR PDB; 6CUU; X-ray; 2.99 A; E=1-99. DR PDB; 6KQD; X-ray; 3.30 A; E/O=1-99. DR PDB; 6KQE; X-ray; 3.30 A; E=1-99. DR PDB; 6KQF; X-ray; 2.45 A; E=1-99. DR PDB; 6KQG; X-ray; 2.78 A; E=1-99. DR PDB; 6KQH; X-ray; 3.18 A; E=1-99. DR PDB; 6KQL; X-ray; 2.89 A; E=1-99. DR PDB; 6KQM; X-ray; 3.20 A; E=1-99. DR PDB; 6KQN; X-ray; 3.49 A; E=1-99. DR PDB; 6L74; X-ray; 3.12 A; E=1-99. DR PDB; 6LTS; X-ray; 3.45 A; E=1-99. DR PDB; 6M6A; EM; 5.00 A; E=1-99. DR PDB; 6M6B; EM; 4.10 A; E=1-99. DR PDB; 6M6C; EM; 3.10 A; E=1-99. DR PDB; 6OVR; X-ray; 2.84 A; E=1-99. DR PDB; 6OVY; X-ray; 3.00 A; E=1-99. DR PDB; 6OW3; X-ray; 2.77 A; E=1-99. DR PDB; 6OY5; X-ray; 3.10 A; E=1-99. DR PDB; 6OY6; X-ray; 3.10 A; E=1-99. DR PDB; 6OY7; X-ray; 3.04 A; E=1-99. DR PDB; 6P70; X-ray; 3.05 A; E=1-99. DR PDB; 6P71; X-ray; 2.92 A; E=1-99. DR PDB; 6WOX; X-ray; 3.14 A; E=1-99. DR PDB; 6WOY; X-ray; 3.00 A; E=1-99. DR PDB; 7EH0; X-ray; 2.81 A; E=1-99. DR PDB; 7EH1; X-ray; 2.90 A; E=1-99. DR PDB; 7EH2; X-ray; 3.34 A; E/O=1-99. DR PDB; 7MLB; X-ray; 3.60 A; E=1-99. DR PDB; 7MLI; X-ray; 3.60 A; E=1-99. DR PDB; 7MLJ; X-ray; 3.75 A; E=1-99. DR PDB; 7RDQ; EM; 3.00 A; E=1-99. DR PDB; 8HSG; EM; 3.20 A; K=1-99. DR PDB; 8HSH; EM; 3.40 A; K=1-99. DR PDB; 8HSL; EM; 5.80 A; K=1-99. DR PDB; 8HSR; EM; 4.00 A; K=1-99. DR PDBsum; 1IW7; -. DR PDBsum; 1SMY; -. DR PDBsum; 1ZYR; -. DR PDBsum; 2A68; -. DR PDBsum; 2A69; -. DR PDBsum; 2A6E; -. DR PDBsum; 2A6H; -. DR PDBsum; 2BE5; -. DR PDBsum; 2CW0; -. DR PDBsum; 2O5I; -. DR PDBsum; 2O5J; -. DR PDBsum; 2PPB; -. DR PDBsum; 3AOH; -. DR PDBsum; 3AOI; -. DR PDBsum; 3DXJ; -. DR PDBsum; 3EQL; -. DR PDBsum; 3WOD; -. DR PDBsum; 4G7H; -. DR PDBsum; 4G7O; -. DR PDBsum; 4G7Z; -. DR PDBsum; 4GZY; -. DR PDBsum; 4GZZ; -. DR PDBsum; 4MQ9; -. DR PDBsum; 4OIN; -. DR PDBsum; 4OIO; -. DR PDBsum; 4OIP; -. DR PDBsum; 4OIQ; -. DR PDBsum; 4OIR; -. DR PDBsum; 4Q4Z; -. DR PDBsum; 4Q5S; -. DR PDBsum; 4WQS; -. DR PDBsum; 4WQT; -. DR PDBsum; 5D4C; -. DR PDBsum; 5D4D; -. DR PDBsum; 5D4E; -. DR PDBsum; 5E17; -. DR PDBsum; 5E18; -. DR PDBsum; 5I2D; -. DR PDBsum; 5TMC; -. DR PDBsum; 5TMF; -. DR PDBsum; 5VO8; -. DR PDBsum; 5VOI; -. DR PDBsum; 5X21; -. DR PDBsum; 5X22; -. DR PDBsum; 5XJ0; -. DR PDBsum; 6ASG; -. DR PDBsum; 6CUU; -. DR PDBsum; 6KQD; -. DR PDBsum; 6KQE; -. DR PDBsum; 6KQF; -. DR PDBsum; 6KQG; -. DR PDBsum; 6KQH; -. DR PDBsum; 6KQL; -. DR PDBsum; 6KQM; -. DR PDBsum; 6KQN; -. DR PDBsum; 6L74; -. DR PDBsum; 6LTS; -. DR PDBsum; 6M6A; -. DR PDBsum; 6M6B; -. DR PDBsum; 6M6C; -. DR PDBsum; 6OVR; -. DR PDBsum; 6OVY; -. DR PDBsum; 6OW3; -. DR PDBsum; 6OY5; -. DR PDBsum; 6OY6; -. DR PDBsum; 6OY7; -. DR PDBsum; 6P70; -. DR PDBsum; 6P71; -. DR PDBsum; 6WOX; -. DR PDBsum; 6WOY; -. DR PDBsum; 7EH0; -. DR PDBsum; 7EH1; -. DR PDBsum; 7EH2; -. DR PDBsum; 7MLB; -. DR PDBsum; 7MLI; -. DR PDBsum; 7MLJ; -. DR PDBsum; 7RDQ; -. DR PDBsum; 8HSG; -. DR PDBsum; 8HSH; -. DR PDBsum; 8HSL; -. DR PDBsum; 8HSR; -. DR AlphaFoldDB; Q8RQE7; -. DR EMDB; EMD-24424; -. DR EMDB; EMD-30117; -. DR EMDB; EMD-30118; -. DR EMDB; EMD-30119; -. DR EMDB; EMD-34996; -. DR EMDB; EMD-34997; -. DR EMDB; EMD-35000; -. DR EMDB; EMD-35004; -. DR SMR; Q8RQE7; -. DR DIP; DIP-47008N; -. DR IntAct; Q8RQE7; 5. DR DrugBank; DB08266; Methyl [(1E,5R)-5-{3-[(2E,4E)-2,5-dimethyl-2,4-octadienoyl]-2,4-dioxo-3,4-dihydro-2H-pyran-6-yl}hexylidene]carbamate. DR DrugBank; DB08226; Myxopyronin B. DR EnsemblBacteria; BAD71384; BAD71384; BAD71384. DR GeneID; 3169896; -. DR KEGG; ttj:TTHA1561; -. DR PATRIC; fig|300852.9.peg.1532; -. DR eggNOG; COG1758; Bacteria. DR HOGENOM; CLU_2319205_0_0_0; -. DR BRENDA; 2.7.7.6; 2305. DR EvolutionaryTrace; Q8RQE7; -. DR Proteomes; UP000000532; Chromosome. 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:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR Gene3D; 3.90.940.10; -; 1. DR HAMAP; MF_00366; RNApol_bact_RpoZ; 1. DR InterPro; IPR003716; DNA-dir_RNA_pol_omega. DR InterPro; IPR006110; Pol_omega/Rpo6/RPB6. DR InterPro; IPR036161; RPB6/omega-like_sf. DR NCBIfam; TIGR00690; rpoZ; 1. DR Pfam; PF01192; RNA_pol_Rpb6; 1. DR SMART; SM01409; RNA_pol_Rpb6; 1. DR SUPFAM; SSF63562; RPB6/omega subunit-like; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase; KW Reference proteome; Transcription; Transferase. FT CHAIN 1..99 FT /note="DNA-directed RNA polymerase subunit omega" FT /id="PRO_0000129004" FT CONFLICT 61 FT /note="V -> E (in Ref. 1; BAB89402)" FT /evidence="ECO:0000305" FT CONFLICT 92 FT /note="L -> I (in Ref. 1; BAB89402)" FT /evidence="ECO:0000305" FT CONFLICT 95 FT /note="V -> G (in Ref. 1; BAB89402)" FT /evidence="ECO:0000305" FT HELIX 6..12 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 16..32 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 33..37 FT /evidence="ECO:0007829|PDB:6KQF" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 61..68 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 69..71 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 74..80 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 84..92 FT /evidence="ECO:0007829|PDB:2A6H" SQ SEQUENCE 99 AA; 11517 MW; 1D213933B0B98965 CRC64; MAEPGIDKLF GMVDSKYRLT VVVAKRAQQL LRHGFKNTVL EPEERPKMQT LEGLFDDPNA VTWAMKELLT GRLVFGENLV PEDRLQKEME RLYPVEREE //