RPOZ_THET8
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 03-AUG-2022, entry version 127.
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}; OrderedLocusNames=TTHA1561;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; 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}.
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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; 5XJ0; X-ray; 4.00 A; E=1-99.
DR PDB; 6ASG; X-ray; 3.80 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; 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 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; 5XJ0; -.
DR PDBsum; 6ASG; -.
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; 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 AlphaFoldDB; Q8RQE7; -.
DR SMR; Q8RQE7; -.
DR DIP; DIP-47008N; -.
DR IntAct; Q8RQE7; 5.
DR STRING; 300852.55772943; -.
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 OMA; NPVTWAM; -.
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:transcription, DNA-templated; 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 Pfam; PF01192; RNA_pol_Rpb6; 1.
DR SMART; SM01409; RNA_pol_Rpb6; 1.
DR SUPFAM; SSF63562; SSF63562; 1.
DR TIGRFAMs; TIGR00690; rpoZ; 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
