RPOE_STRU0
ID RPOE_STRU0 Reviewed; 188 AA.
AC B9DTJ7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=SUB0325;
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J;
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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; AM946015; CAR40896.1; -; Genomic_DNA.
DR RefSeq; WP_012657867.1; NC_012004.1.
DR AlphaFoldDB; B9DTJ7; -.
DR SMR; B9DTJ7; -.
DR STRING; 218495.SUB0325; -.
DR EnsemblBacteria; CAR40896; CAR40896; SUB0325.
DR GeneID; 58022808; -.
DR KEGG; sub:SUB0325; -.
DR eggNOG; COG3343; Bacteria.
DR HOGENOM; CLU_116648_0_0_9; -.
DR OMA; TWGLRSW; -.
DR OrthoDB; 2007175at2; -.
DR Proteomes; UP000000449; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..188
FT /note="Probable DNA-directed RNA polymerase subunit delta"
FT /id="PRO_1000133452"
FT DOMAIN 14..83
FT /note="HTH HARE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01261"
FT REGION 117..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 188 AA; 21811 MW; AB30567AF809660D CRC64;
MKLDIFAGQE KSELSMIEVA RAILEERGRD NEVYFSDLVN DIQTFLGKSD ADIRQALPFF
YTDLNTDGSF IPLGDNKWGL RSWYAIDEID EEIITLEDEE DGAPKRKKKR VNAFMDGDED
AIDYSDDDPE DEDFTEETSD VEYDEEDPDD EKSEVESYDS ELNEIIPEDD IEEVEINEED
DEDDEEEE