ID   RPOZ_THEAQ              Reviewed;          99 AA.
AC   Q9EVV4;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=DNA-directed RNA polymerase subunit omega;
DE            Short=RNAP omega subunit;
DE            EC=2.7.7.6;
DE   AltName: Full=RNA polymerase omega subunit;
DE   AltName: Full=Transcriptase subunit omega;
GN   Name=rpoZ;
OS   Thermus aquaticus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11114902; DOI=10.1128/jb.183.1.71-76.2001;
RA   Minakhin L., Nechaev S., Campbell E.A., Severinov K.;
RT   "Recombinant Thermus aquaticus RNA polymerase, a new tool for structure-
RT   based analysis of transcription.";
RL   J. Bacteriol. 183:71-76(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, AND
RP   3D-STRUCTURE MODELING.
RX   PubMed=11158566; DOI=10.1073/pnas.98.3.892;
RA   Minakhin L., Bhagat S., Brunning A., Campbell E.A., Darst S.A.,
RA   Ebright R.H., Severinov K.;
RT   "Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase
RT   subunit RPB6 are sequence, structural, and functional homologs and promote
RT   RNA polymerase assembly.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:892-897(2001).
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.
CC       {ECO:0000269|PubMed:11158566}.
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: 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   -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC       {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   EMBL; AJ295839; CAC15848.1; -; Genomic_DNA.
DR   RefSeq; WP_053767593.1; NZ_LHCI01000106.1.
DR   PDB; 1HQM; X-ray; 3.30 A; E=1-99.
DR   PDB; 1I6V; X-ray; 3.30 A; E=1-99.
DR   PDB; 1L9U; X-ray; 4.00 A; E/N=1-99.
DR   PDB; 1L9Z; X-ray; 6.50 A; E=1-99.
DR   PDB; 1YNJ; X-ray; 3.20 A; K=1-99.
DR   PDB; 1YNN; X-ray; 3.30 A; K=1-99.
DR   PDB; 4XLN; X-ray; 4.00 A; E/K=1-99.
DR   PDB; 4XLP; X-ray; 4.00 A; E/K=1-99.
DR   PDB; 4XLQ; X-ray; 4.60 A; E/K=1-99.
DR   PDB; 4XLR; X-ray; 4.30 A; E/K=1-99.
DR   PDB; 4XLS; X-ray; 4.01 A; E/K=1-99.
DR   PDB; 5TJG; X-ray; 2.60 A; E=1-99.
DR   PDBsum; 1HQM; -.
DR   PDBsum; 1I6V; -.
DR   PDBsum; 1L9U; -.
DR   PDBsum; 1L9Z; -.
DR   PDBsum; 1YNJ; -.
DR   PDBsum; 1YNN; -.
DR   PDBsum; 4XLN; -.
DR   PDBsum; 4XLP; -.
DR   PDBsum; 4XLQ; -.
DR   PDBsum; 4XLR; -.
DR   PDBsum; 4XLS; -.
DR   PDBsum; 5TJG; -.
DR   AlphaFoldDB; Q9EVV4; -.
DR   SMR; Q9EVV4; -.
DR   EvolutionaryTrace; Q9EVV4; -.
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; Direct protein sequencing; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Transcription; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11158566"
FT   CHAIN           2..99
FT                   /note="DNA-directed RNA polymerase subunit omega"
FT                   /id="PRO_0000129002"
FT   HELIX           6..11
FT                   /evidence="ECO:0007829|PDB:5TJG"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:5TJG"
FT   HELIX           16..32
FT                   /evidence="ECO:0007829|PDB:5TJG"
FT   TURN            33..37
FT                   /evidence="ECO:0007829|PDB:5TJG"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:5TJG"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1YNJ"
FT   HELIX           60..68
FT                   /evidence="ECO:0007829|PDB:5TJG"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:5TJG"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:5TJG"
FT   HELIX           82..89
FT                   /evidence="ECO:0007829|PDB:5TJG"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:1YNN"
SQ   SEQUENCE   99 AA;  11625 MW;  1BEC4908DB29CBF6 CRC64;
     MAEPGIDKLF GMVDSKYRLT VVVAKRAQQL LRHRFKNTVL EPEERPKMRT LEGLYDDPNA
     VTWAMKELLT GRLFFGENLV PEDRLQKEME RLYPTEEEA