RPOZ_STRP3
ID RPOZ_STRP3 Reviewed; 104 AA.
AC P0DF36; P68841; P82577;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
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; OrderedLocusNames=SpyM3_1374;
OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=198466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-595 / MGAS315;
RX PubMed=12122206; DOI=10.1073/pnas.152298499;
RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT encoded toxins, the high-virulence phenotype, and clone emergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(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=AAM79981.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014074; AAM79981.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P0DF36; -.
DR SMR; P0DF36; -.
DR EnsemblBacteria; AAM79981; AAM79981; SpyM3_1374.
DR KEGG; spg:SpyM3_1374; -.
DR HOGENOM; CLU_125406_0_0_9; -.
DR OMA; AHEIDKY; -.
DR Proteomes; UP000000564; 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..104
FT /note="DNA-directed RNA polymerase subunit omega"
FT /id="PRO_0000128996"
SQ SEQUENCE 104 AA; 11705 MW; FD6FDF3D852CC7F1 CRC64;
MLKPSIDTLL DKVPSKYSLV ILQAKRAHEL EAGATPTQEF KSVKSTLQAL EEIESGNVVI
HPDPSAKREA VRAKIEAERL AKEEEERKIK EQIAKEKEEE GEKI