GFH1_THET8
ID GFH1_THET8 Reviewed; 156 AA.
AC Q5SJG6; Q8VQD5;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-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=TTHA1042;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND GENE NAME.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND INTERACTION WITH RNAP.
RX PubMed=14712703; DOI=10.1016/s0076-6879(03)71016-7;
RA Laptenko O., Borukhov S.;
RT "Biochemical assays of Gre factors of Thermus thermophilus.";
RL Methods Enzymol. 371:219-232(2003).
RN [4]
RP CRYSTALLIZATION.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=16511259; DOI=10.1107/s1744309105040297;
RA Perederina A.A., Vassylyeva M.N., Berezin I.A., Svetlov V.,
RA Artsimovitch I., Vassylyev D.G.;
RT "Cloning, expression, purification, crystallization and initial
RT crystallographic analysis of transcription elongation factors GreB from
RT Escherichia coli and Gfh1 from Thermus thermophilus.";
RL Acta Crystallogr. F 62:44-46(2006).
RN [5]
RP CRYSTALLIZATION, AND INTERACTION WITH RNAP.
RX PubMed=20057074; DOI=10.1107/s1744309109049215;
RA Tagami S., Sekine S., Kumarevel T., Yamamoto M., Yokoyama S.;
RT "Crystallization and preliminary X-ray crystallographic analysis of Thermus
RT thermophilus transcription elongation complex bound to Gfh1.";
RL Acta Crystallogr. F 66:64-68(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC, AND FUNCTION.
RX PubMed=16298991; DOI=10.1074/jbc.c500405200;
RA Symersky J., Perederina A., Vassylyeva M.N., Svetlov V., Artsimovitch I.,
RA Vassylyev D.G.;
RT "Regulation through the RNA polymerase secondary channel. Structural and
RT functional variability of the coiled-coil transcription factors.";
RL J. Biol. Chem. 281:1309-1312(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (4.10 ANGSTROMS) IN COMPLEX WITH RNAP.
RX PubMed=21124318; DOI=10.1038/nature09573;
RA Tagami S., Sekine S., Kumarevel T., Hino N., Murayama Y., Kamegamori S.,
RA Yamamoto M., Sakamoto K., Yokoyama S.;
RT "Crystal structure of bacterial RNA polymerase bound with a transcription
RT inhibitor protein.";
RL Nature 468:978-982(2010).
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:11606592, ECO:0000269|PubMed:14712703,
CC ECO:0000269|PubMed:16298991}.
CC -!- SUBUNIT: Interacts with RNAP. {ECO:0000269|PubMed:14712703,
CC ECO:0000269|PubMed:16298991, ECO:0000269|PubMed:20057074,
CC ECO:0000269|PubMed:21124318}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GreA/GreB family. {ECO:0000305}.
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DR EMBL; AF456235; AAL57612.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70865.1; -; Genomic_DNA.
DR RefSeq; WP_011228396.1; NC_006461.1.
DR RefSeq; YP_144308.1; NC_006461.1.
DR PDB; 2EUL; X-ray; 2.40 A; A/B/C/D=1-156.
DR PDB; 3AOH; X-ray; 4.10 A; X/Y/Z=1-156.
DR PDB; 3AOI; X-ray; 4.30 A; X/Y/Z=1-156.
DR PDB; 4WQT; X-ray; 4.40 A; X/Y/Z=1-156.
DR PDBsum; 2EUL; -.
DR PDBsum; 3AOH; -.
DR PDBsum; 3AOI; -.
DR PDBsum; 4WQT; -.
DR AlphaFoldDB; Q5SJG6; -.
DR SMR; Q5SJG6; -.
DR DIP; DIP-59216N; -.
DR IntAct; Q5SJG6; 4.
DR STRING; 300852.55772424; -.
DR EnsemblBacteria; BAD70865; BAD70865; BAD70865.
DR GeneID; 3168268; -.
DR KEGG; ttj:TTHA1042; -.
DR PATRIC; fig|300852.9.peg.1022; -.
DR eggNOG; COG0782; Bacteria.
DR HOGENOM; CLU_101379_2_1_0; -.
DR OMA; ILQEQME; -.
DR PhylomeDB; Q5SJG6; -.
DR EvolutionaryTrace; Q5SJG6; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Metal-binding; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..156
FT /note="Transcription inhibitor protein Gfh1"
FT /id="PRO_0000422249"
FT COILED 1..74
FT /evidence="ECO:0000255"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16298991"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16298991"
FT CONFLICT 146
FT /note="R -> K (in Ref. 1; AAL57612)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:2EUL"
FT HELIX 9..38
FT /evidence="ECO:0007829|PDB:2EUL"
FT HELIX 46..71
FT /evidence="ECO:0007829|PDB:2EUL"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2EUL"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2EUL"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:2EUL"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:2EUL"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:2EUL"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2EUL"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2EUL"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:2EUL"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:2EUL"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:2EUL"
SQ SEQUENCE 156 AA; 17183 MW; 2B7BB05B0E8ECE14 CRC64;
MAREVKLTKA GYERLMQQLE RERERLQEAT KILQELMESS DDYDDSGLEA AKQEKARIEA
RIDSLEDILS RAVILEEGSG EVIGLGSVVE LEDPLSGERL SVQVVSPAEA NVLDTPMKIS
DASPMGKALL GHRVGDVLSL DTPKGRREFR VVAIHG
