RPOZ_ACTP7
ID RPOZ_ACTP7 Reviewed; 93 AA.
AC B3GZ78;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=APP7_1912;
OS Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=537457;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP76;
RA Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA Tegetmeyer H., Singh M., Gerlach G.F.;
RT "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL Submitted (JUN-2008) 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: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; CP001091; ACE62564.1; -; Genomic_DNA.
DR RefSeq; WP_005599441.1; NC_010939.1.
DR AlphaFoldDB; B3GZ78; -.
DR SMR; B3GZ78; -.
DR EnsemblBacteria; ACE62564; ACE62564; APP7_1912.
DR GeneID; 66258591; -.
DR KEGG; apa:APP7_1912; -.
DR HOGENOM; CLU_125406_5_3_6; -.
DR OMA; NVDNRFQ; -.
DR BioCyc; APLE537457:APP7_RS09985-MON; -.
DR Proteomes; UP000001226; 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..93
FT /note="DNA-directed RNA polymerase subunit omega"
FT /id="PRO_1000121181"
SQ SEQUENCE 93 AA; 10376 MW; 0E620ACC5A1F0580 CRC64;
MARVTVQEAA DKIGNRFDLI LTAARRARQL QLHAREPLVP EENDKPTVIA LREIEKGLIN
GQIMDQLENN DAIQQEVAEQ EAISFLADVQ ANA