ID   GFH1_THEAQ              Reviewed;         157 AA.
AC   Q8VQD7;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Transcription inhibitor protein Gfh1;
DE   AltName: Full=Anti-cleavage anti-GreA transcription factor;
DE   AltName: Full=Gre factor homolog 1;
GN   Name=gfh1;
OS   Thermus aquaticus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND GENE NAME.
RX   PubMed=11606592; DOI=10.1074/jbc.m108737200;
RA   Hogan B.P., Hartsch T., Erie D.A.;
RT   "Transcript cleavage by Thermus thermophilus RNA polymerase. Effects of
RT   GreA and anti-GreA factors.";
RL   J. Biol. Chem. 277:967-975(2002).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS), FUNCTION, INTERACTION WITH RNAP,
RP   AND DOMAIN.
RX   PubMed=16337964; DOI=10.1016/j.jmb.2005.10.083;
RA   Lamour V., Hogan B.P., Erie D.A., Darst S.A.;
RT   "Crystal structure of Thermus aquaticus Gfh1, a Gre-factor paralog that
RT   inhibits rather than stimulates transcript cleavage.";
RL   J. Mol. Biol. 356:179-188(2006).
CC   -!- FUNCTION: Inhibits all catalytic activities of RNA polymerase (RNAP) by
CC       partially occluding its substrate-binding site and preventing NTP
CC       binding. {ECO:0000305|PubMed:11606592, ECO:0000305|PubMed:16337964}.
CC   -!- SUBUNIT: Interacts with RNAP. {ECO:0000305|PubMed:16337964}.
CC   -!- DOMAIN: Inhibitory activity is regulated via a pH-induced
CC       conformational change of the structure. At pH above 7, Gfh1 is in an
CC       inactive flipped orientation that prevents binding to RNAP. At lower
CC       pH, Gfh1 switches to an active orientation, which enables binding to
CC       RNAP and inhibitory activity (Probable). {ECO:0000305|PubMed:16337964}.
CC   -!- SIMILARITY: Belongs to the GreA/GreB family. {ECO:0000305}.
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DR   EMBL; AF456233; AAL57610.1; -; Genomic_DNA.
DR   PDB; 2ETN; X-ray; 3.30 A; A/B/C=1-157.
DR   PDBsum; 2ETN; -.
DR   AlphaFoldDB; Q8VQD7; -.
DR   SMR; Q8VQD7; -.
DR   EvolutionaryTrace; Q8VQD7; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0070063; F:RNA polymerase binding; IEA:InterPro.
DR   GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro.
DR   Gene3D; 1.10.287.180; -; 1.
DR   Gene3D; 3.10.50.30; -; 1.
DR   InterPro; IPR036953; GreA/GreB_C_sf.
DR   InterPro; IPR018151; TF_GreA/GreB_CS.
DR   InterPro; IPR001437; Tscrpt_elong_fac_GreA/B_C.
DR   InterPro; IPR023459; Tscrpt_elong_fac_GreA/B_fam.
DR   InterPro; IPR022691; Tscrpt_elong_fac_GreA/B_N.
DR   InterPro; IPR036805; Tscrpt_elong_fac_GreA/B_N_sf.
DR   PANTHER; PTHR30437; PTHR30437; 1.
DR   Pfam; PF01272; GreA_GreB; 1.
DR   Pfam; PF03449; GreA_GreB_N; 1.
DR   PIRSF; PIRSF006092; GreA_GreB; 1.
DR   SUPFAM; SSF46557; SSF46557; 1.
DR   PROSITE; PS00830; GREAB_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Transcription; Transcription regulation.
FT   CHAIN           1..157
FT                   /note="Transcription inhibitor protein Gfh1"
FT                   /id="PRO_0000422247"
FT   COILED          1..74
FT                   /evidence="ECO:0000255"
FT   HELIX           9..36
FT                   /evidence="ECO:0007829|PDB:2ETN"
FT   HELIX           47..68
FT                   /evidence="ECO:0007829|PDB:2ETN"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:2ETN"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:2ETN"
FT   STRAND          88..92
FT                   /evidence="ECO:0007829|PDB:2ETN"
FT   TURN            94..96
FT                   /evidence="ECO:0007829|PDB:2ETN"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:2ETN"
FT   HELIX           107..109
FT                   /evidence="ECO:0007829|PDB:2ETN"
FT   STRAND          111..120
FT                   /evidence="ECO:0007829|PDB:2ETN"
FT   HELIX           124..129
FT                   /evidence="ECO:0007829|PDB:2ETN"
FT   STRAND          137..141
FT                   /evidence="ECO:0007829|PDB:2ETN"
FT   STRAND          143..151
FT                   /evidence="ECO:0007829|PDB:2ETN"
SQ   SEQUENCE   157 AA;  17228 MW;  F705CA040959ED46 CRC64;
     MAREVKLTKA GYERLMKQLE QERERLQEAT KILQELMESS DDYDDSGLEA AKQEKARIEA
     RIDSLEDVLS RAVILEEGTG EVIGLGSVVE LEDPATGERL SVQVVSPAEA SVLENPMKIS
     DASPMGKALL GHRVGDVLSL DTPKGKKEFR VVAIHGR