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InterPro: IPR000551 HTH transcriptional regulator, MerR

Protein matches Help

UniProtKB

Matches:

9780 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR000551 HTH_MerR

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00376	MerR	9370
PRINTS	PR00040	HTHMERR	3924
PROSITE pattern	PS00552	HTH_MERR_1	2657
PROSITE profile	PS50937	HTH_MERR_2	8607
SMART	SM00422	HTH_MERR	8264
Signatures in BioMart

InterPro Relationships Help

Parent

IPR009061 Putative DNA binding

Found in

IPR010093 Excisionase/Xis, DNA-binding
IPR010211 Redox-sensitive transcriptional activator SoxR
IPR011788 Zn(II)-responsive transcriptional regulator
IPR011789 Cu(I)-responsive transcriptional regulator
IPR011791 Cd(II)/Pb(II)-responsive transcriptional regulator
IPR011794 Hg(II)-responsive transcriptional regulator
IPR011797 Mercuric resistence transcriptional repressor protein MerD
IPR017818 Plasmid partitioning protein, RepA

GO Term annotation Help

Process

GO:0006355 regulation of transcription, DNA-dependent

Function

GO:0003700 transcription factor activity

InterPro annotation

Entry Details in BioMart

Abstract

The many bacterial transcription regulation proteins which bind DNA through a 'helix-turn-helix' motif can be classified into subfamilies on the basis of sequence similarities. One of these is the MerR subfamily. MerR, which is found in many bacterial species mediates the mercuric-dependent induction of the mercury resistance operon. In the absence of mercury merR represses transcription by binding tightly, as a dimer, to the 'mer' operator region; when mercury is present the dimeric complex binds a single ion and becomes a potent transcriptional activator, while remaining bound to the mer site. Members of the family include the mercuric resistance operon regulatory protein merR; Bacillus subtilis bltR and bmrR; Bacillus glnR; Streptomyces coelicolor hspR; Bradyrhizobium japonicum nolA; Escherichia coli superoxide response regulator soxR; and Streptomyces lividans transcriptional activator tipA [1, 2, 3, 4, 5, 6]. Other members include hypothetical proteins from E. coli, B. subtilis and Haemophilus influenzae. Within this family, the HTH motif is situated towards the N terminus.

Structural links Help

PDB - click here

SCOP: a.6.1.3

CATH: 1.10.1660.10

Database links Help

PDBe-motif: PS00552

PROSITE doc: PDOC00477

PANDIT: PF00376

Blocks: IPB000551

Pfam Clan: CL0123.14

AC	CL0123.14
ID	HTH
DE	Helix-turn-helix clan
PF00046	IPR001356	Homeobox
PF00126	IPR000847	HTH transcriptional regulator, LysR
PF00165	IPR000005	Helix-turn-helix, AraC type
PF00196	IPR000792	Transcription regulator LuxR, C-terminal
PF00325	IPR001808	HTH transcriptional regulator, Crp
PF00356	IPR000843	HTH transcriptional regulator, LacI
PF00376	IPR000551	HTH transcriptional regulator, MerR
PF00392	IPR000524	HTH transcriptional regulator, GntR
PF00440	IPR001647	Transcriptional regulator, TetR-like, DNA-binding, bacterial/archaeal
PF00486	IPR001867	Signal transduction response regulator, C-terminal
PF01022	IPR001845	HTH transcriptional regulator, ArsR
PF01047	IPR000835	HTH transcriptional regulator, MarR
PF01316	IPR020900	Arginine repressor, DNA-binding domain
PF01325	IPR001367	Iron dependent repressor
PF01371	IPR000831	Trp repressor
PF01381	IPR001387	Helix-turn-helix type 3
PF01418	IPR000281	Helix-turn-helix protein RpiR
PF01475	IPR002481	Ferric-uptake regulator
PF01527	IPR002514	Transposase IS3/IS911
PF01638	IPR002577	Helix-turn-helix, HxlR type
PF01726	IPR006199	LexA, DNA-binding domain
PF01978	IPR002831	Transcriptional regulator TrmB
PF02001	IPR002852	Uncharacterised protein family UPF0251
PF02002	IPR002853	Transcription factor TFIIE, alpha subunit
PF02082	IPR000944	Transcriptional regulator, Rrf2
PF02295	IPR000607	Double-stranded RNA-specific adenosine deaminase (DRADA)
PF02319	IPR003316	Transcription factor E2F/dimerisation partner (TDP)
PF02796	IPR006120	Resolvase, helix-turn-helix domain
PF02954	IPR002197	Helix-turn-helix, Fis-type
PF03444	IPR005104	Protein of unknown function DUF293, archaea
PF03551	IPR005149	Transcriptional regulator PadR N-terminal-like
PF03811	IPR003220	Insertion element protein
PF03965	IPR005650	Penicillinase repressor
PF04218	IPR006695	Centromere protein Cenp-B, DNA-binding domain 1
PF04297	IPR007394	Putative helix-turn-helix protein, YlxM/p13-like
PF04545	IPR007630	RNA polymerase sigma-70 region 4
PF04552	IPR007634	RNA polymerase sigma factor 54, DNA-binding
PF04703	IPR006793	FaeA-like protein
PF04967	IPR007050	Bacterio-opsin activator, HTH
PF05043	IPR007737	M trans-acting positive regulator
PF05225	IPR007889	Helix-turn-helix, Psq
PF05269	IPR007933	Bacteriophage CII
PF05331	IPR007995	Protein of unknown function DUF742
PF05584	IPR008848	Plasmid regulator, Sulfolobaceae
PF05732	IPR008813	Firmicute plasmid replication
PF05920	IPR008422	Mating-type protein, fungi
PF05930	IPR010260	Prophage CP4-57 regulatory
PF06056	IPR010332	ATPase terminase subunit, putative
PF06163	IPR010382	Protein of unknown function DUF977, bacterial
PF06530	IPR010534	Phage antitermination Q-like
PF06971	IPR009718	Rex DNA-binding, C-terminal
PF07022	IPR010744	Bacteriophage CI repressor
PF07106	IPR010776	Tat binding protein 1-interacting
PF07453	IPR010896	Nuclease-associated modular DNA-binding 1
PF07638	IPR011517	RNA polymerase sigma-70 ECF-like
PF07750	IPR011681	GcrA cell cycle regulator
PF07825	IPR012884	Excisionase-like
PF07848	IPR012906	PaaX-like, N-terminal
PF07900	IPR012872	Protein of unknown function DUF1670
PF08100	IPR012967	Plant methyltransferase dimerisation
PF08220	IPR001034	HTH transcriptional regulator, DeoR N-terminal
PF08221	IPR013197	RNA polymerase III subunit RPC82-related, helix-turn-helix
PF08222	IPR013198	GTP-sensing helix-turn-helix, CodY, C-terminal
PF08279	IPR013196	Helix-turn-helix, type 11
PF08280	IPR013199	Helix-turn-helix Mga, DNA-binding trans-acting positive regulator
PF08281	IPR013249	RNA polymerase sigma factor 70, region 4 type 2
PF08299	IPR013159	Chromosomal replication initiator, DnaA C-terminal
PF08461	IPR013668	Ribonuclease R winged-helix domain
PF08914	IPR015010	Rap1 Myb
PF09202	IPR015285	RIO2 kinase, winged helix, N-terminal
PF09339	IPR005471	Transcriptional regulator IclR, N-terminal

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000551

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O22001 Gene 36 protein

P0A4T9 HTH-type transcriptional activator tipA

Q55963 Uncharacterized HTH-type transcriptional regulator slr0701

Q60329 Uncharacterized protein MJ0014

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR012925	TipAS antibiotic-recognition
IPR009061	Putative DNA binding
IPR010093	Excisionase/Xis, DNA-binding
IPR000551	HTH transcriptional regulator, MerR
IPR006119	Resolvase, N-terminal
IPR015358	Transcription regulator MerR, DNA binding
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Holmes DJ, Caso JL, Thompson CJ. Autogenous transcriptional activation of a thiostrepton-induced gene in Streptomyces lividans. EMBO J. 12 3183-91 1993 [PubMed: 7688297] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=7688297
2.	Helmann JD, Wang Y, Mahler I, Walsh CT. Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons. J. Bacteriol. 171 222-9 1989 [PubMed: 2492496] http://jb.asm.org/cgi/content/abstract/171/1/222
3.	Ahmed M, Lyass L, Markham PN, Taylor SS, Vazquez-Laslop N, Neyfakh AA. Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated. J. Bacteriol. 177 3904-10 1995 [PubMed: 7608059] http://jb.asm.org/cgi/content/abstract/177/14/3904
4.	Nakano Y, Kimura K. Purification and characterization of a repressor for the Bacillus cereus glnRA operon. J. Biochem. 109 223-8 1991 [PubMed: 1677938] http://jb.oxfordjournals.org/cgi/content/abstract/109/2/223
5.	Sadowsky MJ, Cregan PB, Gottfert M, Sharma A, Gerhold D, Rodriguez-Quinones F, Keyser HH, Hennecke H, Stacey G. The Bradyrhizobium japonicum nolA gene and its involvement in the genotype-specific nodulation of soybeans. Proc. Natl. Acad. Sci. U.S.A. 88 637-41 1991 [PubMed: 1988958] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=1988958
6.	Helmann JD, Ballard BT, Walsh CT. The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer. Science 247 946-8 1990 [PubMed: 2305262] http://www.sciencemag.org/cgi/content/abstract/247/4945/946

Additional Reading Open in usermanual
	Godsey MH, Baranova NN, Neyfakh AA, Brennan RG. Crystal structure of MtaN, a global multidrug transporter gene activator. J. Biol. Chem. 276 2001 47178-84 [PubMed: 11581256] http://dx.doi.org/10.1074/jbc.M105819200
	Newberry KJ, Brennan RG. The structural mechanism for transcription activation by MerR family member multidrug transporter activation, N terminus. J. Biol. Chem. 279 2004 20356-62 [PubMed: 14985361] http://dx.doi.org/10.1074/jbc.M400960200
	Newberry KJ, Huffman JL, Miller MC, Vazquez-Laslop N, Neyfakh AA, Brennan RG. Structures of BmrR-drug complexes reveal a rigid multidrug binding pocket and transcription activation through tyrosine expulsion. J. Biol. Chem. 283 2008 26795-804 [PubMed: 18658145] http://dx.doi.org/10.1074/jbc.M804191200
	Wu J, Weiss B. Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coli. J. Bacteriol. 173 1991 2864-71 [PubMed: 1708380] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1708380
	Brown NL, Stoyanov JV, Kidd SP, Hobman JL. The MerR family of transcriptional regulators. FEMS Microbiol. Rev. 27 2003 145-63 [PubMed: 12829265] http://dx.doi.org/10.1016/S0168-6445(03)00051-2
	Changela A, Chen K, Xue Y, Holschen J, Outten CE, O'Halloran TV, Mondragon A. Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR. Science 301 2003 1383-7 [PubMed: 12958362] http://dx.doi.org/10.1126/science.1085950
	Heldwein EE, Brennan RG. Crystal structure of the transcription activator BmrR bound to DNA and a drug. Nature 409 2001 378-82 [PubMed: 11201751] http://dx.doi.org/10.1038/35053138

InterPro 23.1