TFE_SACS2
ID TFE_SACS2 Reviewed; 178 AA.
AC Q980M5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 123.
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=SSO0266;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, AND INTERACTION WITH TBP AND RNA POLYMERASE.
RX PubMed=11258705; DOI=10.1093/embo-reports/kve021;
RA Bell S.D., Brinkman A.B., van der Oost J., Jackson S.P.;
RT "The archaeal TFIIEalpha homologue facilitates transcription initiation by
RT enhancing TATA-box recognition.";
RL EMBO Rep. 2:133-138(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-110, AND DOMAIN.
RX PubMed=13679366; DOI=10.1074/jbc.m307874200;
RA Meinhart A., Blobel J., Cramer P.;
RT "An extended winged helix domain in general transcription factor E/IIE
RT alpha.";
RL J. Biol. Chem. 278:48267-48274(2003).
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:11258705}.
CC -!- SUBUNIT: Monomer (Probable). Interaction with RNA polymerase subunits
CC RpoF and RpoE is necessary for Tfe stimulatory transcription activity.
CC Able to interact with Tbp and RNA polymerase in the absence of DNA
CC promoter. Interacts both with the preinitiation and elongation
CC complexes (By similarity). {ECO:0000250, ECO:0000305}.
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; AE006641; AAK40605.1; -; Genomic_DNA.
DR PIR; F90168; F90168.
DR RefSeq; WP_009990539.1; NC_002754.1.
DR PDB; 1Q1H; X-ray; 2.90 A; A=1-110.
DR PDBsum; 1Q1H; -.
DR AlphaFoldDB; Q980M5; -.
DR SMR; Q980M5; -.
DR STRING; 273057.SSO0266; -.
DR EnsemblBacteria; AAK40605; AAK40605; SSO0266.
DR GeneID; 44129239; -.
DR KEGG; sso:SSO0266; -.
DR PATRIC; fig|273057.12.peg.261; -.
DR eggNOG; arCOG04270; Archaea.
DR HOGENOM; CLU_100097_0_0_2; -.
DR InParanoid; Q980M5; -.
DR OMA; DSGWLTY; -.
DR PhylomeDB; Q980M5; -.
DR EvolutionaryTrace; Q980M5; -.
DR Proteomes; UP000001974; 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 PANTHER; PTHR13097; PTHR13097; 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 PROSITE; PS51344; HTH_TFE_IIE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..178
FT /note="Transcription factor E"
FT /id="PRO_0000318948"
FT DOMAIN 4..88
FT /note="HTH TFE/IIEalpha-type"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:1Q1H"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:1Q1H"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1Q1H"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:1Q1H"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:1Q1H"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1Q1H"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1Q1H"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1Q1H"
SQ SEQUENCE 178 AA; 21173 MW; F7A734DA4030D40F CRC64;
MVNAEDLFIN LAKSLLGDDV IDVLRILLDK GTEMTDEEIA NQLNIKVNDV RKKLNLLEEQ
GFVSYRKTRD KDSGWFIYYW KPNIDQINEI LLNRKRLILD KLKTRLEYEK NNTFFICPQD
NSRYSFEEAF ENEFKCLKCG SQLTYYDTDK IKSFLEQKIR QIEEEIDKET KLGANKNH
