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RPOZ_CLOD6
ID   RPOZ_CLOD6              Reviewed;          88 AA.
AC   Q182S6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=CD630_25871;
GN   ORFNames=CD2587A;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ69477.1; -; Genomic_DNA.
DR   RefSeq; WP_003431167.1; NZ_CP010905.2.
DR   RefSeq; YP_001089104.1; NC_009089.1.
DR   PDB; 7L7B; EM; 3.26 A; E=1-88.
DR   PDBsum; 7L7B; -.
DR   AlphaFoldDB; Q182S6; -.
DR   SMR; Q182S6; -.
DR   STRING; 272563.CD630_25871; -.
DR   ChEMBL; CHEMBL2363852; -.
DR   DrugCentral; Q182S6; -.
DR   EnsemblBacteria; CAJ69477; CAJ69477; CD630_25871.
DR   GeneID; 66354988; -.
DR   KEGG; cdf:CD630_25871; -.
DR   KEGG; pdc:CDIF630_02841; -.
DR   PATRIC; fig|272563.120.peg.2729; -.
DR   eggNOG; COG1758; Bacteria.
DR   OMA; KRARMLT; -.
DR   PhylomeDB; Q182S6; -.
DR   BioCyc; PDIF272563:G12WB-2744-MON; -.
DR   PRO; PR:Q182S6; -.
DR   Proteomes; UP000001978; 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   1: Evidence at protein level;
KW   3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..88
FT                   /note="DNA-directed RNA polymerase subunit omega"
FT                   /id="PRO_1000005914"
SQ   SEQUENCE   88 AA;  10198 MW;  B26955EA7DE3C1B2 CRC64;
     MLKPSINEVL EKIDNRYYLV GTVSKRARKL IDGEEPYVSN KTKEKPVCVA TKEVASGKIT
     YRLLTEEEIE IEEARHHAEQ HQQISEEE
 
 
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