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Protein

Transcription inhibitor protein Gfh1

Gene

gfh1

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits all catalytic activities of RNA polymerase (RNAP) by partially occluding its substrate-binding site and preventing NTP binding.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi20 – 201Zinc1 Publication
Metal bindingi24 – 241Zinc1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1074-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription inhibitor protein Gfh1
Alternative name(s):
Anti-cleavage anti-GreA transcription factor
Gre factor homolog 1
Gene namesi
Name:gfh1
Ordered Locus Names:TTHA1042
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156Transcription inhibitor protein Gfh1PRO_0000422249Add
BLAST

Interactioni

Subunit structurei

Interacts with RNAP.4 Publications

Protein-protein interaction databases

DIPiDIP-59216N.
STRINGi300852.TTHA1042.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Helixi9 – 3830Combined sources
Helixi46 – 7126Combined sources
Beta strandi72 – 743Combined sources
Beta strandi88 – 936Combined sources
Turni94 – 974Combined sources
Beta strandi98 – 1058Combined sources
Turni107 – 1093Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi118 – 1203Combined sources
Helixi124 – 1296Combined sources
Beta strandi137 – 1404Combined sources
Beta strandi147 – 1548Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EULX-ray2.40A/B/C/D1-156[»]
3AOHX-ray4.10X/Y/Z1-156[»]
3AOIX-ray4.30X/Y/Z1-156[»]
4WQTX-ray4.40X/Y/Z1-156[»]
ProteinModelPortaliQ5SJG6.
SMRiQ5SJG6. Positions 1-156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SJG6.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 7474Sequence analysisAdd
BLAST

Domaini

Inhibitory activity is regulated via a pH-induced conformational change of the structure. At pH above 7, Gfh1 is in an inactive flipped orientation that prevents binding to RNAP. At lower pH, Gfh1 switches to an active orientation, which enables binding to RNAP and inhibitory activity (By similarity).By similarity

Sequence similaritiesi

Belongs to the GreA/GreB family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG4105RTX. Bacteria.
COG0782. LUCA.
HOGENOMiHOG000241145.
KOiK03624.
OMAiAFMETRI.
OrthoDBiEOG686NQ9.
PhylomeDBiQ5SJG6.

Family and domain databases

Gene3Di1.10.287.180. 1 hit.
3.10.50.30. 1 hit.
InterProiIPR018151. TF_GreA/GreB_CS.
IPR001437. Tscrpt_elong_fac_GreA/B_C.
IPR023459. Tscrpt_elong_fac_GreA/B_fam.
IPR022691. Tscrpt_elong_fac_GreA/B_N.
[Graphical view]
PfamiPF01272. GreA_GreB. 1 hit.
PF03449. GreA_GreB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF006092. GreA_GreB. 1 hit.
SUPFAMiSSF46557. SSF46557. 1 hit.
PROSITEiPS00830. GREAB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SJG6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAREVKLTKA GYERLMQQLE RERERLQEAT KILQELMESS DDYDDSGLEA
60 70 80 90 100
AKQEKARIEA RIDSLEDILS RAVILEEGSG EVIGLGSVVE LEDPLSGERL
110 120 130 140 150
SVQVVSPAEA NVLDTPMKIS DASPMGKALL GHRVGDVLSL DTPKGRREFR

VVAIHG
Length:156
Mass (Da):17,183
Last modified:December 21, 2004 - v1
Checksum:i2B7BB05B0E8ECE14
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461R → K in AAL57612 (PubMed:11606592).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF456235 Genomic DNA. Translation: AAL57612.1.
AP008226 Genomic DNA. Translation: BAD70865.1.
RefSeqiWP_011228396.1. NC_006461.1.
YP_144308.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70865; BAD70865; BAD70865.
GeneIDi3168268.
KEGGittj:TTHA1042.
PATRICi23957044. VBITheThe93045_1022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF456235 Genomic DNA. Translation: AAL57612.1.
AP008226 Genomic DNA. Translation: BAD70865.1.
RefSeqiWP_011228396.1. NC_006461.1.
YP_144308.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EULX-ray2.40A/B/C/D1-156[»]
3AOHX-ray4.10X/Y/Z1-156[»]
3AOIX-ray4.30X/Y/Z1-156[»]
4WQTX-ray4.40X/Y/Z1-156[»]
ProteinModelPortaliQ5SJG6.
SMRiQ5SJG6. Positions 1-156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59216N.
STRINGi300852.TTHA1042.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70865; BAD70865; BAD70865.
GeneIDi3168268.
KEGGittj:TTHA1042.
PATRICi23957044. VBITheThe93045_1022.

Phylogenomic databases

eggNOGiENOG4105RTX. Bacteria.
COG0782. LUCA.
HOGENOMiHOG000241145.
KOiK03624.
OMAiAFMETRI.
OrthoDBiEOG686NQ9.
PhylomeDBiQ5SJG6.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1074-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SJG6.

Family and domain databases

Gene3Di1.10.287.180. 1 hit.
3.10.50.30. 1 hit.
InterProiIPR018151. TF_GreA/GreB_CS.
IPR001437. Tscrpt_elong_fac_GreA/B_C.
IPR023459. Tscrpt_elong_fac_GreA/B_fam.
IPR022691. Tscrpt_elong_fac_GreA/B_N.
[Graphical view]
PfamiPF01272. GreA_GreB. 1 hit.
PF03449. GreA_GreB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF006092. GreA_GreB. 1 hit.
SUPFAMiSSF46557. SSF46557. 1 hit.
PROSITEiPS00830. GREAB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Transcript cleavage by Thermus thermophilus RNA polymerase. Effects of GreA and anti-GreA factors."
    Hogan B.P., Hartsch T., Erie D.A.
    J. Biol. Chem. 277:967-975(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, GENE NAME.
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "Biochemical assays of Gre factors of Thermus thermophilus."
    Laptenko O., Borukhov S.
    Methods Enzymol. 371:219-232(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RNAP.
  4. "Cloning, expression, purification, crystallization and initial crystallographic analysis of transcription elongation factors GreB from Escherichia coli and Gfh1 from Thermus thermophilus."
    Perederina A.A., Vassylyeva M.N., Berezin I.A., Svetlov V., Artsimovitch I., Vassylyev D.G.
    Acta Crystallogr. F 62:44-46(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
    Strain: HB8 / ATCC 27634 / DSM 579.
  5. "Crystallization and preliminary X-ray crystallographic analysis of Thermus thermophilus transcription elongation complex bound to Gfh1."
    Tagami S., Sekine S., Kumarevel T., Yamamoto M., Yokoyama S.
    Acta Crystallogr. F 66:64-68(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, INTERACTION WITH RNAP.
  6. "Regulation through the RNA polymerase secondary channel. Structural and functional variability of the coiled-coil transcription factors."
    Symersky J., Perederina A., Vassylyeva M.N., Svetlov V., Artsimovitch I., Vassylyev D.G.
    J. Biol. Chem. 281:1309-1312(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION.
  7. "Crystal structure of bacterial RNA polymerase bound with a transcription inhibitor protein."
    Tagami S., Sekine S., Kumarevel T., Hino N., Murayama Y., Kamegamori S., Yamamoto M., Sakamoto K., Yokoyama S.
    Nature 468:978-982(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.10 ANGSTROMS) IN COMPLEX WITH RNAP.

Entry informationi

Entry nameiGFH1_THET8
AccessioniPrimary (citable) accession number: Q5SJG6
Secondary accession number(s): Q8VQD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2013
Last sequence update: December 21, 2004
Last modified: November 11, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.