ID A0A0K0ILL4_9FIRM Unreviewed; 181 AA.
AC A0A0K0ILL4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ORFNames=WH51_16155 {ECO:0000313|EMBL:KKE77769.1};
OS Bacilli bacterium VT-13-104.
OC Bacteria; Bacillota; Bacilli.
OX NCBI_TaxID=1637974 {ECO:0000313|EMBL:KKE77769.1, ECO:0000313|Proteomes:UP000034981};
RN [1] {ECO:0000313|Proteomes:UP000034981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VT-13-104 {ECO:0000313|Proteomes:UP000034981};
RA Tetz V., Tetz G.;
RT "Bacilli bacterium VT-13-104.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKE77769.1}.
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DR EMBL; LAZH01000073; KKE77769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K0ILL4; -.
DR PATRIC; fig|1637974.4.peg.3391; -.
DR OrthoDB; 401223at2; -.
DR Proteomes; UP000034981; Unassembled WGS sequence.
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:UP000034981};
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 14..81
FT /note="HTH HARE-type"
FT /evidence="ECO:0000259|PROSITE:PS51913"
FT REGION 89..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..181
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 181 AA; 21642 MW; E9DEB17E014A2167 CRC64;
MSLKDYSPEQ IENMSMLELA SIILKEEKKA LHFKDVFDKV AEVKGFSEAE KEEKIAQFYT
DLNVDGRFTT LGSNMWGLKR WYPIEQADEE VHTPKKKKKK ATKKKRKEEE IDEEEDFEEE
DDLLEDEDID EVFDDEEEDL DEDDEELDPD LDEFDDFDED EEEIDEEFDD EELDDEEEEE
K
//
