ID A0A2X4WPK4_9NOCA Unreviewed; 100 AA.
AC A0A2X4WPK4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=DNA-directed RNA polymerase subunit omega {ECO:0000256|ARBA:ARBA00013725, ECO:0000256|HAMAP-Rule:MF_00366};
DE Short=RNAP omega subunit {ECO:0000256|HAMAP-Rule:MF_00366};
DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418, ECO:0000256|HAMAP-Rule:MF_00366};
DE AltName: Full=RNA polymerase omega subunit {ECO:0000256|HAMAP-Rule:MF_00366};
DE AltName: Full=Transcriptase subunit omega {ECO:0000256|ARBA:ARBA00029924, ECO:0000256|HAMAP-Rule:MF_00366};
GN Name=rpoZ {ECO:0000256|HAMAP-Rule:MF_00366,
GN ECO:0000313|EMBL:SQI28895.1};
GN ORFNames=NCTC10994_00648 {ECO:0000313|EMBL:SQI28895.1};
OS Rhodococcus coprophilus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=38310 {ECO:0000313|EMBL:SQI28895.1, ECO:0000313|Proteomes:UP000249091};
RN [1] {ECO:0000313|EMBL:SQI28895.1, ECO:0000313|Proteomes:UP000249091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10994 {ECO:0000313|EMBL:SQI28895.1,
RC ECO:0000313|Proteomes:UP000249091};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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:0000256|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:0000256|ARBA:ARBA00024550,
CC ECO:0000256|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:0000256|ARBA:ARBA00025935, ECO:0000256|HAMAP-Rule:MF_00366}.
CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC {ECO:0000256|ARBA:ARBA00006711, ECO:0000256|HAMAP-Rule:MF_00366}.
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DR EMBL; LS483468; SQI28895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X4WPK4; -.
DR STRING; 1219011.GCA_001895045_00368; -.
DR KEGG; rcr:NCTC10994_00648; -.
DR Proteomes; UP000249091; Chromosome 1.
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:DNA-templated transcription; 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 NCBIfam; TIGR00690; rpoZ; 1.
DR PANTHER; PTHR34476; DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA; 1.
DR PANTHER; PTHR34476:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA; 1.
DR Pfam; PF01192; RNA_pol_Rpb6; 1.
DR SMART; SM01409; RNA_pol_Rpb6; 1.
DR SUPFAM; SSF63562; RPB6/omega subunit-like; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00366};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00366}; Reference proteome {ECO:0000313|Proteomes:UP000249091};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00366};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00366}.
SQ SEQUENCE 100 AA; 10995 MW; 2454E6D99C9D1B84 CRC64;
MSSMQAAAID LEGNALPVYD TPLGITNPPI DELLERASSK YALVIYSAKR ARQINDYYNQ
LGDGILEYVG PLVEPGLQEK PLSIALREIH ADLLEHTEGE
//
