ID   RPOZ_SALPK              Reviewed;          91 AA.
AC   B5BI24;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=SSPA3356;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(2009).
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; FM200053; CAR61622.1; -; Genomic_DNA.
DR   RefSeq; WP_000135058.1; NC_011147.1.
DR   AlphaFoldDB; B5BI24; -.
DR   SMR; B5BI24; -.
DR   GeneID; 64726409; -.
DR   GeneID; 67517126; -.
DR   KEGG; sek:SSPA3356; -.
DR   HOGENOM; CLU_125406_5_3_6; -.
DR   OMA; NVDNRFQ; -.
DR   Proteomes; UP000001869; 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; Transcription;
KW   Transferase.
FT   CHAIN           1..91
FT                   /note="DNA-directed RNA polymerase subunit omega"
FT                   /id="PRO_1000121270"
SQ   SEQUENCE   91 AA;  10237 MW;  4DE7E81EF670D887 CRC64;
     MARVTVQDAV EKIGNRFDLV LVAARRARQM QVGGKDPLVP EENDKTTVIA LREIEEGLIN
     NQILDVRERQ EQQEQEAAEL QAVTAIAEGR R