ID   RPOE_STRPG              Reviewed;         191 AA.
AC   A2RCL2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Probable DNA-directed RNA polymerase subunit delta {ECO:0000255|HAMAP-Rule:MF_00357};
DE   AltName: Full=RNAP delta factor {ECO:0000255|HAMAP-Rule:MF_00357};
GN   Name=rpoE {ECO:0000255|HAMAP-Rule:MF_00357}; OrderedLocusNames=SpyM50243;
OS   Streptococcus pyogenes serotype M5 (strain Manfredo).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=160491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Manfredo;
RX   PubMed=17012393; DOI=10.1128/jb.01227-06;
RA   Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA   Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA   Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT   "Complete genome of acute rheumatic fever-associated serotype M5
RT   Streptococcus pyogenes strain Manfredo.";
RL   J. Bacteriol. 189:1473-1477(2007).
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. {ECO:0000255|HAMAP-Rule:MF_00357}.
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. {ECO:0000255|HAMAP-Rule:MF_00357}.
CC   -!- SIMILARITY: Belongs to the RpoE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00357}.
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DR   EMBL; AM295007; CAM29585.1; -; Genomic_DNA.
DR   RefSeq; WP_002988147.1; NC_009332.1.
DR   AlphaFoldDB; A2RCL2; -.
DR   SMR; A2RCL2; -.
DR   GeneID; 57853292; -.
DR   KEGG; spf:SpyM50243; -.
DR   HOGENOM; CLU_116648_0_0_9; -.
DR   OMA; TWGLRSW; -.
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_0000303144"
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