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InterPro: IPR014757 Transcriptional regulator IclR, C-terminal

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4702 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR014757 Transcript_reg_IclR_C

Secondary

IPR000285 , IPR005471

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01614	IclR	4485
PROSITE profile	PS51078	ICLR_ED	4691
Signatures in BioMart

InterPro Relationships Help

Found in

IPR012794 Beta-ketoadipate transcriptional regulator, PcaR/PcaU/PobR

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 subfamilies, called 'iclR', groups several proteins including:

gylR, a possible activator protein for the gylABX glycerol operon in Streptomyces.

iclR, the repressor of the acetate operon (also known as glyoxylate bypass operon) in Escherichia coli and Salmonella typhimurium.

These proteins have a Helix-Turn-Helix motif at the N terminus that is similar to that of other DNA-binding proteins [1].

Structural links Help

PDB - click here

SCOP: a.4.5.33 , d.110.2.2

CATH: 1.10.10.10 , 1.20.5.640 , 3.30.450.40

Database links Help

PROSITE doc: PDOC00807

PANDIT: PF01614

Pfam Clan: CL0161.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR014757

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0ACN4 HTH-type transcriptional repressor allR

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005471	Transcriptional regulator IclR, N-terminal
IPR014757	Transcriptional regulator IclR, C-terminal
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Reverchon S, Nasser W, Robert-Baudouy J. Characterization of kdgR, a gene of Erwinia chrysanthemi that regulates pectin degradation. Mol. Microbiol. 5 2203-16 1991 [PubMed: 1840643] http://dx.doi.org/10.1111/j.1365-2958.1991.tb02150.x

Additional Reading Open in usermanual
	Molina-Henares AJ, Krell T, Eugenia Guazzaroni M, Segura A, Ramos JL. Members of the IclR family of bacterial transcriptional regulators function as activators and/or repressors. FEMS Microbiol. Rev. 30 2006 157-86 [PubMed: 16472303] http://dx.doi.org/10.1111/j.1574-6976.2005.00008.x
	Zhang RG, Kim Y, Skarina T, Beasley S, Laskowski R, Arrowsmith C, Edwards A, Joachimiak A, Savchenko A. Crystal structure of Thermotoga maritima 0065, a member of the IclR transcriptional factor family. J. Biol. Chem. 277 2002 19183-90 [PubMed: 11877432] http://dx.doi.org/10.1074/jbc.M112171200
	Galinier A, Bleicher F, Negre D, Perriere G, Duclos B, Cozzone AJ, Cortay JC. Primary structure of the intergenic region between aceK and iclR in the Escherichia coli chromosome. Gene 97 1991 149-50 [PubMed: 1995429] http://dx.doi.org/10.1016/0378-1119(91)90024-6
	Walker JR, Altamentova S, Ezersky A, Lorca G, Skarina T, Kudritska M, Ball LJ, Bochkarev A, Savchenko A. Structural and biochemical study of effector molecule recognition by the E.coli glyoxylate and allantoin utilization regulatory protein AllR. J. Mol. Biol. 358 2006 810-28 [PubMed: 16546208] http://dx.doi.org/10.1016/j.jmb.2006.02.034
	Smith CP, Chater KF. Structure and regulation of controlling sequences for the Streptomyces coelicolor glycerol operon. J. Mol. Biol. 204 1988 569-80 [PubMed: 3225846] http://dx.doi.org/10.1016/0022-2836(88)90356-7
	Lorca GL, Ezersky A, Lunin VV, Walker JR, Altamentova S, Evdokimova E, Vedadi M, Bochkarev A, Savchenko A. Glyoxylate and pyruvate are antagonistic effectors of the Escherichia coli IclR transcriptional regulator. J. Biol. Chem. 282 2007 16476-91 [PubMed: 17426033] http://dx.doi.org/10.1074/jbc.M610838200

InterPro 24.0