ID   TFE_ARCFU               Reviewed;         177 AA.
AC   O29501;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Transcription factor E {ECO:0000255|HAMAP-Rule:MF_01909};
DE            Short=TFE {ECO:0000255|HAMAP-Rule:MF_01909};
DE   AltName: Full=TFIIE subunit alpha homolog {ECO:0000255|HAMAP-Rule:MF_01909};
DE   AltName: Full=Transcription initiation factor TFIIE {ECO:0000255|HAMAP-Rule:MF_01909};
GN   Name=tfe {ECO:0000255|HAMAP-Rule:MF_01909}; OrderedLocusNames=AF_0757;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- FUNCTION: Transcription factor that plays a role in the activation of
CC       archaeal genes transcribed by RNA polymerase. Facilitates transcription
CC       initiation by enhancing TATA-box recognition by TATA-box-binding
CC       protein (Tbp), and transcription factor B (Tfb) and RNA polymerase
CC       recruitment. Not absolutely required for transcription in vitro, but
CC       particularly important in cases where Tbp or Tfb function is not
CC       optimal. It dynamically alters the nucleic acid-binding properties of
CC       RNA polymerases by stabilizing the initiation complex and destabilizing
CC       elongation complexes. Seems to translocate with the RNA polymerase
CC       following initiation and acts by binding to the non template strand of
CC       the transcription bubble in elongation complexes. {ECO:0000255|HAMAP-
CC       Rule:MF_01909}.
CC   -!- SUBUNIT: Monomer. Interaction with RNA polymerase subunits RpoF and
CC       RpoE is necessary for Tfe stimulatory transcription activity. Able to
CC       interact with Tbp and RNA polymerase in the absence of DNA promoter.
CC       Interacts both with the preinitiation and elongation complexes.
CC       {ECO:0000255|HAMAP-Rule:MF_01909}.
CC   -!- DOMAIN: The winged helix domain is involved in binding to DNA in the
CC       preinitiation complex. {ECO:0000255|HAMAP-Rule:MF_01909}.
CC   -!- SIMILARITY: Belongs to the TFE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01909}.
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DR   EMBL; AE000782; AAB90479.1; -; Genomic_DNA.
DR   PIR; E69344; E69344.
DR   RefSeq; WP_010878260.1; NC_000917.1.
DR   AlphaFoldDB; O29501; -.
DR   SMR; O29501; -.
DR   STRING; 224325.AF_0757; -.
DR   EnsemblBacteria; AAB90479; AAB90479; AF_0757.
DR   GeneID; 24794355; -.
DR   KEGG; afu:AF_0757; -.
DR   eggNOG; arCOG04270; Archaea.
DR   HOGENOM; CLU_100097_0_0_2; -.
DR   OMA; DSGWLTY; -.
DR   OrthoDB; 75288at2157; -.
DR   PhylomeDB; O29501; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_01909; TFE_arch; 1.
DR   InterPro; IPR016481; TF_E_archaea.
DR   InterPro; IPR039997; TFE.
DR   InterPro; IPR017919; TFIIE/TFIIEa_HTH.
DR   InterPro; IPR002853; TFIIE_asu.
DR   InterPro; IPR024550; TFIIEa/SarR/Rpc3_HTH_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   InterPro; IPR013137; Znf_TFIIB.
DR   PANTHER; PTHR13097; PTHR13097; 1.
DR   Pfam; PF08271; TF_Zn_Ribbon; 1.
DR   Pfam; PF02002; TFIIE_alpha; 1.
DR   PIRSF; PIRSF006373; TF_E_archaea; 1.
DR   SMART; SM00531; TFIIE; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   TIGRFAMs; TIGR00373; TIGR00373; 1.
DR   PROSITE; PS51344; HTH_TFE_IIE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..177
FT                   /note="Transcription factor E"
FT                   /id="PRO_0000326588"
FT   DOMAIN          9..91
FT                   /note="HTH TFE/IIEalpha-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01909"
SQ   SEQUENCE   177 AA;  20373 MW;  2944586B0E37B3B5 CRC64;
     MKAETTTGVE ELLNELVGRA AGEVGLILFS LGIEGEFTDD QLSLELGIEI NEIRKALFAL
     YEIGLADYVR RRDDETGWME YYWRINYDKA LDVLKRELEK TAKKLREKIE AETSTIYYIC
     PNMCVKVSYN DAMELNFTCP RCGAMLDYLD CSKAIEKIEE EVRRIEEILE SLDKNSG