GFH1_THET2
ID GFH1_THET2 Reviewed; 156 AA.
AC Q72JT8;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 113.
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; OrderedLocusNames=TT_C0680;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), FUNCTION, INTERACTION WITH RNAP,
RP DOMAIN, AND MUTAGENESIS OF LEU-75; GLU-77; GLY-135 AND GLY-156.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=16628221; DOI=10.1038/sj.emboj.7601094;
RA Laptenko O., Kim S.S., Lee J., Starodubtseva M., Cava F., Berenguer J.,
RA Kong X.P., Borukhov S.;
RT "pH-dependent conformational switch activates the inhibitor of
RT transcription elongation.";
RL EMBO J. 25:2131-2141(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:0000269|PubMed:16628221}.
CC -!- SUBUNIT: Interacts with RNAP. {ECO:0000269|PubMed:16628221}.
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. {ECO:0000269|PubMed:16628221}.
CC -!- SIMILARITY: Belongs to the GreA/GreB family. {ECO:0000305}.
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DR EMBL; AE017221; AAS81028.1; -; Genomic_DNA.
DR RefSeq; WP_011173122.1; NC_005835.1.
DR PDB; 2F23; X-ray; 1.60 A; A/B=1-156.
DR PDBsum; 2F23; -.
DR AlphaFoldDB; Q72JT8; -.
DR SMR; Q72JT8; -.
DR STRING; 262724.TT_C0680; -.
DR EnsemblBacteria; AAS81028; AAS81028; TT_C0680.
DR KEGG; tth:TT_C0680; -.
DR eggNOG; COG0782; Bacteria.
DR HOGENOM; CLU_101379_2_1_0; -.
DR OMA; ILQEQME; -.
DR OrthoDB; 1536415at2; -.
DR EvolutionaryTrace; Q72JT8; -.
DR Proteomes; UP000000592; Chromosome.
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..156
FT /note="Transcription inhibitor protein Gfh1"
FT /id="PRO_0000422248"
FT COILED 1..74
FT /evidence="ECO:0000255"
FT MUTAGEN 75
FT /note="L->C: Lacks inhibitory activity and is insensitive
FT to pH; when associated with C-135."
FT /evidence="ECO:0000269|PubMed:16628221"
FT MUTAGEN 77
FT /note="E->C: Strong inhibitory activity and insensitivity
FT to pH; when associated with C-156."
FT /evidence="ECO:0000269|PubMed:16628221"
FT MUTAGEN 135
FT /note="G->C: Lacks inhibitory activity and is insensitive
FT to pH; when associated with C-75."
FT /evidence="ECO:0000269|PubMed:16628221"
FT MUTAGEN 156
FT /note="G->C: Strong inhibitory activity and insensitivity
FT to pH; when associated with C-77."
FT /evidence="ECO:0000269|PubMed:16628221"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:2F23"
FT HELIX 9..37
FT /evidence="ECO:0007829|PDB:2F23"
FT HELIX 46..71
FT /evidence="ECO:0007829|PDB:2F23"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2F23"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2F23"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2F23"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:2F23"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2F23"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:2F23"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:2F23"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:2F23"
FT STRAND 145..155
FT /evidence="ECO:0007829|PDB:2F23"
SQ SEQUENCE 156 AA; 17155 MW; 2B7BAF660E8ECE14 CRC64;
MAREVKLTKA GYERLMQQLE RERERLQEAT KILQELMESS DDYDDSGLEA AKQEKARIEA
RIDSLEDILS RAVILEEGSG EVIGLGSVVE LEDPLSGERL SVQVVSPAEA NVLDTPMKIS
DASPMGKALL GHRVGDVLSL DTPKGKREFR VVAIHG
