ID D2BPA8_LACLK Unreviewed; 187 AA.
AC D2BPA8;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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:ADA64383.1};
GN OrderedLocusNames=LLKF_0628 {ECO:0000313|EMBL:ADA64383.1};
OS Lactococcus lactis subsp. lactis (strain KF147).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=684738 {ECO:0000313|EMBL:ADA64383.1, ECO:0000313|Proteomes:UP000001886};
RN [1] {ECO:0000313|EMBL:ADA64383.1, ECO:0000313|Proteomes:UP000001886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF147 {ECO:0000313|EMBL:ADA64383.1,
RC ECO:0000313|Proteomes:UP000001886};
RX PubMed=18039825; DOI=10.1128/AEM.01850-07;
RA Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D.,
RA van Hylckama Vlieg J.E.;
RT "Genome-scale genotype-phenotype matching of two Lactococcus lactis
RT isolates from plants identifies mechanisms of adaptation to the plant
RT niche.";
RL Appl. Environ. Microbiol. 74:424-436(2008).
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; CP001834; ADA64383.1; -; Genomic_DNA.
DR RefSeq; WP_012897344.1; NC_013656.1.
DR AlphaFoldDB; D2BPA8; -.
DR GeneID; 69712642; -.
DR KEGG; llk:LLKF_0628; -.
DR HOGENOM; CLU_116648_0_0_9; -.
DR Proteomes; UP000001886; 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};
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 97..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..187
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 187 AA; 21357 MW; 2A8E25A1BCE84DC7 CRC64;
MKITALEGQK ISELSMIEVA HALLEQNGKE MQFSEIIRAI QDYLEKSDDE IKASISRFYT
EINTDGSFIP LGNNIWALRS WYAIDEIDEE VIALDEIEDE EEEKPAKKRK KVNAFGIEDE
IDPEDEEGAK ETTEEDMSYD TQAEDEDKDD VAAYDAELAE VELDNVDEEV DIDVEDDEDD
SDDTDED
//