ID   TFE_METAC               Reviewed;         167 AA.
AC   Q8TJB7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 103.
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=MA_3871;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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; AE010299; AAM07222.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TJB7; -.
DR   SMR; Q8TJB7; -.
DR   STRING; 188937.MA_3871; -.
DR   EnsemblBacteria; AAM07222; AAM07222; MA_3871.
DR   KEGG; mac:MA_3871; -.
DR   HOGENOM; CLU_100097_0_0_2; -.
DR   InParanoid; Q8TJB7; -.
DR   OMA; DSGWLTY; -.
DR   PhylomeDB; Q8TJB7; -.
DR   Proteomes; UP000002487; 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; 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   PROSITE; PS51344; HTH_TFE_IIE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..167
FT                   /note="Transcription factor E"
FT                   /id="PRO_0000326608"
FT   DOMAIN          8..90
FT                   /note="HTH TFE/IIEalpha-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01909"
SQ   SEQUENCE   167 AA;  19514 MW;  1D5492254A2F264F CRC64;
     MNTLVDLNDK VIRGYLISLV GEEGLRMIEE MPEGEVTDEE IAAKTGVLLN TVRRTLFILY
     ENKFAICRRE RDSNSGWLTY LWHLDFSDVE HQLMREKKKL LRNLKTRLEF EENNVFYVCP
     QGCVRLLFDE ATETEFLCPM CGEDLVYYDN SRFVSALKKR VDALSSV