ID   RPOE_STRP3              Reviewed;         191 AA.
AC   P0DF34; P58053; P66720;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Probable DNA-directed RNA polymerase subunit delta;
DE   AltName: Full=RNAP delta factor;
GN   Name=rpoE; OrderedLocusNames=SpyM3_1633;
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: Participates in both the initiation and recycling phases of
CC       transcription. In the presence of the delta subunit, RNAP displays an
CC       increased specificity of transcription, a decreased affinity for
CC       nucleic acids, and an increased efficiency of RNA synthesis because of
CC       enhanced recycling (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: RNAP is composed of a core of 2 alpha, a beta and a beta'
CC       subunits. The core is associated with a delta subunit and one of
CC       several sigma factors (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RpoE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM80240.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014074; AAM80240.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002988147.1; NC_004070.1.
DR   AlphaFoldDB; P0DF34; -.
DR   SMR; P0DF34; -.
DR   PRIDE; P0DF34; -.
DR   EnsemblBacteria; AAM80240; AAM80240; SpyM3_1633.
DR   GeneID; 57853292; -.
DR   KEGG; spg:SpyM3_1633; -.
DR   HOGENOM; CLU_116648_0_0_9; -.
DR   OMA; TWGLRSW; -.
DR   Proteomes; UP000000564; Chromosome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.10.1250; -; 1.
DR   HAMAP; MF_00357; RNApol_bact_RpoE; 1.
DR   InterPro; IPR007759; Asxl_HARE-HTH.
DR   InterPro; IPR038087; RNAP_delta_N_dom_sf.
DR   InterPro; IPR029757; RpoE.
DR   Pfam; PF05066; HARE-HTH; 1.
DR   TIGRFAMs; TIGR04567; RNAP_delt_lowGC; 1.
DR   PROSITE; PS51913; HTH_HARE; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW   Transferase.
FT   CHAIN           1..191
FT                   /note="Probable DNA-directed RNA polymerase subunit delta"
FT                   /id="PRO_0000204332"
FT   DOMAIN          14..83
FT                   /note="HTH HARE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01261"
FT   REGION          118..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..191
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   191 AA;  22265 MW;  D1781EFA0BC6926C CRC64;
     MKLDVFAGQE KSELSMIEVA RAILEERGRD NEMYFSDLVN EIQNYLGKSD AGIRHALPFF
     YTDLNTDGSF IPLGENKWGL RSWYAIDEID EEIITLEEDE DGAQKRKKKR VNAFMDGDED
     AIDYRDDDPE DEDFTEESAE VEYDEEDPDD EKSEVESYDS ELNEIIPEDD FEEVDINEED
     EEDEEDEEPV L