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Database: UniProt
Entry: A3CQB2_STRSV
LinkDB: A3CQB2_STRSV
Original site: A3CQB2_STRSV 
ID   A3CQB2_STRSV            Unreviewed;       181 AA.
AC   A3CQB2;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Probable DNA-directed RNA polymerase subunit delta {ECO:0000256|HAMAP-Rule:MF_00357};
DE   AltName: Full=RNAP delta factor {ECO:0000256|HAMAP-Rule:MF_00357};
GN   Name=rpoE {ECO:0000256|HAMAP-Rule:MF_00357,
GN   ECO:0000313|EMBL:ABN45367.1};
GN   OrderedLocusNames=SSA_1996 {ECO:0000313|EMBL:ABN45367.1};
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN45367.1, ECO:0000313|Proteomes:UP000002148};
RN   [1] {ECO:0000313|EMBL:ABN45367.1, ECO:0000313|Proteomes:UP000002148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36 {ECO:0000313|EMBL:ABN45367.1,
RC   ECO:0000313|Proteomes:UP000002148};
RX   PubMed=17277061; DOI=10.1128/JB.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(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:0000256|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:0000256|HAMAP-Rule:MF_00357}.
CC   -!- SIMILARITY: Belongs to the RpoE family. {ECO:0000256|ARBA:ARBA00009828,
CC       ECO:0000256|HAMAP-Rule:MF_00357}.
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DR   EMBL; CP000387; ABN45367.1; -; Genomic_DNA.
DR   RefSeq; YP_001035917.1; NC_009009.1.
DR   AlphaFoldDB; A3CQB2; -.
DR   STRING; 388919.SSA_1996; -.
DR   KEGG; ssa:SSA_1996; -.
DR   PATRIC; fig|388919.9.peg.1892; -.
DR   eggNOG; COG3343; Bacteria.
DR   HOGENOM; CLU_116648_0_0_9; -.
DR   OrthoDB; 401223at2; -.
DR   Proteomes; UP000002148; 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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.1250; RNA polymerase, subunit delta, N-terminal domain; 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   NCBIfam; TIGR04567; RNAP_delt_lowGC; 1.
DR   Pfam; PF05066; HARE-HTH; 1.
DR   PROSITE; PS51913; HTH_HARE; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_00357};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00357}; Reference proteome {ECO:0000313|Proteomes:UP000002148};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00357};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00357}.
FT   DOMAIN          1..68
FT                   /note="HTH HARE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51913"
FT   REGION          82..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..181
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   181 AA;  20952 MW;  C4872F5C77326666 CRC64;
     MIEVARAILE ARGRDHEMYF NDLVNEIQNY LEKSNSEIRD ALPLFYTELN VDGSFIPLGD
     NKWGLRSWYA IDEVDEEIIA LEETDEDDAP KKRKKKRVNA FMDGDEDAID YSDDDPEDED
     GYEADPALSY DEENPDDEKN EVEAYDAEIN EIAPDDLGEE VELNEEDDDY SDEDTETEEE
     E
//
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