ID   RPOZ_BRADU              Reviewed;         130 AA.
AC   Q9RH70;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 2.
DT   03-AUG-2022, entry version 121.
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; Synonyms=rnpO; OrderedLocusNames=bll5066;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=USDA 110spc4;
RA   Mueller P., Stingel D.;
RT   "Extended DNA sequencing in the upstream region of sipF in Bradyrhizobium
RT   japonicum.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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 (By similarity).
CC       {ECO:0000250}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF04326.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF065159; AAF04326.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BA000040; BAC50331.1; -; Genomic_DNA.
DR   RefSeq; NP_771706.1; NC_004463.1.
DR   RefSeq; WP_008133017.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q9RH70; -.
DR   SMR; Q9RH70; -.
DR   STRING; 224911.27353331; -.
DR   EnsemblBacteria; BAC50331; BAC50331; BAC50331.
DR   GeneID; 64024830; -.
DR   GeneID; 66401117; -.
DR   KEGG; bja:bll5066; -.
DR   PATRIC; fig|224911.44.peg.4934; -.
DR   eggNOG; COG1758; Bacteria.
DR   HOGENOM; CLU_125406_2_0_5; -.
DR   InParanoid; Q9RH70; -.
DR   OMA; EVDEPEM; -.
DR   PhylomeDB; Q9RH70; -.
DR   PRO; PR:Q9RH70; -.
DR   Proteomes; UP000002526; 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   PANTHER; PTHR34476; PTHR34476; 1.
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   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..130
FT                   /note="DNA-directed RNA polymerase subunit omega"
FT                   /id="PRO_0000128921"
FT   REGION          79..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        37
FT                   /note="T -> K (in Ref. 1; AAF04326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="S -> T (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="E -> Q (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   130 AA;  14354 MW;  AAA0E574D2C56ADF CRC64;
     MARVTVEDCI DKVDNRFDLV LLAAHRARMI SSGSQLTVDR DNDKNPVVSL REIADTTISP
     EDLREELVHS LQKFVEVDEP EPDTVPLIGS AGASVDADDT EVAVERMTEE ELLKGLEGLA
     PPEEQPEEDE