ID   TFE_METTH               Reviewed;         178 AA.
AC   O27705;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 108.
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=MTH_1669;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [2]
RP   FUNCTION, AND MUTAGENESIS OF CYS-137.
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=11160119; DOI=10.1128/jb.183.5.1813-1818.2001;
RA   Hanzelka B.L., Darcy T.J., Reeve J.N.;
RT   "TFE, an archaeal transcription factor in Methanobacterium
RT   thermoautotrophicum related to eucaryal transcription factor TFIIEalpha.";
RL   J. Bacteriol. 183:1813-1818(2001).
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:11160119}.
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}.
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DR   EMBL; AE000666; AAB86141.1; -; Genomic_DNA.
DR   PIR; A69090; A69090.
DR   RefSeq; WP_010877276.1; NC_000916.1.
DR   AlphaFoldDB; O27705; -.
DR   SMR; O27705; -.
DR   STRING; 187420.MTH_1669; -.
DR   EnsemblBacteria; AAB86141; AAB86141; MTH_1669.
DR   GeneID; 24854769; -.
DR   KEGG; mth:MTH_1669; -.
DR   PATRIC; fig|187420.15.peg.1629; -.
DR   HOGENOM; CLU_100097_0_0_2; -.
DR   OMA; DSGWLTY; -.
DR   Proteomes; UP000005223; 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; 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   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..178
FT                   /note="Transcription factor E"
FT                   /id="PRO_0000318946"
FT   DOMAIN          3..89
FT                   /note="HTH TFE/IIEalpha-type"
FT   MUTAGEN         137
FT                   /note="C->A: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:11160119"
SQ   SEQUENCE   178 AA;  21164 MW;  BAD30209977A8E4F CRC64;
     MIDEQVLQEL IHEVITEEEE EEAIPVLECL MKGKVTDEEI SEKTQLKLNI VRRILYRLYD
     AGVASYKRSK DPETQWYTYT WKFEPEKVTE MIKRKHSEIV RKLREALEFE ENNMFFVCVN
     GHYRFTFDEA TEENFTCPEC GSKMEFMDNS EIIQEIKDEL SLYENNGFDS IKTTTINS