ID   TFE_METJA               Reviewed;         173 AA.
AC   Q58187;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Transcription factor E;
DE            Short=TFE;
DE   AltName: Full=TFIIE subunit alpha homolog;
DE   AltName: Full=Transcription initiation factor TFIIE;
GN   Name=tfe; OrderedLocusNames=MJ0777;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=15485836; DOI=10.1074/jbc.c400446200;
RA   Ouhammouch M., Werner F., Weinzierl R.O., Geiduschek E.P.;
RT   "A fully recombinant system for activator-dependent archaeal
RT   transcription.";
RL   J. Biol. Chem. 279:51719-51721(2004).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH TBP AND RNA POLYMERASE.
RX   PubMed=16135821; DOI=10.1128/mcb.25.18.8344-8355.2005;
RA   Werner F., Weinzierl R.O.;
RT   "Direct modulation of RNA polymerase core functions by basal transcription
RT   factors.";
RL   Mol. Cell. Biol. 25:8344-8355(2005).
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.
CC       {ECO:0000269|PubMed:15485836, ECO:0000269|PubMed:16135821}.
CC   -!- SUBUNIT: Monomer (By similarity). Interaction with RNA polymerase
CC       subunits RpoF and RpoE is necessary for Tfe stimulatory transcription
CC       activity. Able to interact with RNA polymerase in the absence of Tbp or
CC       DNA promoter. Interacts both with the preinitiation and elongation
CC       complexes (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The winged helix domain is involved in binding to DNA in the
CC       preinitiation complex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TFE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB98767.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB98767.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q58187; -.
DR   SMR; Q58187; -.
DR   STRING; 243232.MJ_0777; -.
DR   EnsemblBacteria; AAB98767; AAB98767; MJ_0777.
DR   KEGG; mja:MJ_0777; -.
DR   eggNOG; arCOG04270; Archaea.
DR   HOGENOM; CLU_100097_0_0_2; -.
DR   InParanoid; Q58187; -.
DR   OMA; DSGWLTY; -.
DR   PhylomeDB; Q58187; -.
DR   Proteomes; UP000000805; 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:0001113; P:transcription open complex formation at RNA polymerase II promoter; IBA:GO_Central.
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   1: Evidence at protein level;
KW   DNA-binding; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..173
FT                   /note="Transcription factor E"
FT                   /id="PRO_0000107028"
FT   DOMAIN          3..88
FT                   /note="HTH TFE/IIEalpha-type"
SQ   SEQUENCE   173 AA;  20667 MW;  F78759126582C7B6 CRC64;
     MLNDPLVQEV LFNIFEGDEK GFEVIDVLLE KGETTEEEIA KELGVKLNVV RKLLYKLYDA
     RLVDYKRWKD EDTNWYSYTW LPTLEKLPYV VKKKINELIK DLEKKLEFEK NNMFFFCPNC
     NVRFTFEEAM DYGFSCPGCG NMLQEFDNSE LIKDLEEQIK FLKEELKNNP FLK