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0  structures 10047  species 0  interactions 11275  sequences 5  architectures

Family: ArsB (PF02040)

Summary: Arsenical pump membrane protein

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This is the Wikipedia entry entitled "Ars operon". More...

Ars operon Edit Wikipedia article

Anion-transporting ATPase
Symbol ArsA_ATPase
Pfam PF02374
Pfam clan CL0023
SCOP 1f48
TCDB 3.A.4
Symbol ArsB
Pfam PF02040
Pfam clan CL0182
InterPro IPR000802
TCDB 3.A.4
PDB 1rw1 EBI.jpg
yffb (pa3664) protein
Symbol ArsC
Pfam PF03960
Pfam clan CL0172
InterPro IPR006660
SCOP 1i9d
Symbol ArsD
Pfam PF06953
Pfam clan CL0172
InterPro IPR010712

In molecular biology, the ars operon is an operon found in several bacterial taxon. It is required for the detoxification of arsenate, arsenite, and antimonite.[1] This system transports arsenite and antimonite out of the cell. The pump is composed of two polypeptides, the products of the arsA and arsB genes. This two-subunit enzyme produces resistance to arsenite and antimonite. Arsenate, however, must first be reduced to arsenite before it is extruded. A third gene, arsC, expands the substrate specificity to allow for arsenate pumping and resistance. ArsC is an approximately 150-residue arsenate reductase that uses reduced glutathione (GSH) to convert arsenate to arsenite with a redox active cysteine residue in the active site. ArsC forms an active quaternary complex with GSH, arsenate, and glutaredoxin 1 (Grx1). The three ligands must be present simultaneously for reduction to occur.[2]

ArsA and ArsB

ArsA and ArsB form an anion-translocating ATPase.[3] The ArsB protein is distinguished by its overall hydrophobic character, in keeping with its role as a membrane-associated channel. Sequence analysis reveals the presence of 13 putative transmembrane (TM) regions.


The arsC protein structure has been solved.[4] It belongs to the thioredoxin superfamily fold which is defined by a beta-sheet core surrounded by alpha-helices. The active cysteine residue of ArsC is located in the loop between the first beta-strand and the first helix, which is also conserved in the Spx protein and its homologues.

The arsC family also comprises the Spx proteins which are Gram-positive bacterial transcription factors that regulate the transcription of multiple genes in response to disulphide stress.[5]

ArsD and ArsR

ArsD is a trans-acting repressor of the arsRDABC operon that confers resistance to arsenicals and antimonials in Escherichia coli. It possesses two-pairs of vicinal cysteine residues, Cys(12)-Cys(13) and Cys(112)-Cys(113), that potentially form separate binding sites for the metalloids that trigger dissociation of ArsD from the operon. However, as a homodimer it has four vicinal cysteine pairs.[6] The ArsD family consists of several bacterial arsenical resistance operon trans-acting repressor ArsD proteins.

ArsR is a trans-acting regulatory protein. It acts as a repressor on the arsRDABC operon when no arsenic is present in the cell. When arsenic is present in the cell ArsR will lose affinity for the operator and RNA polymerase can transcribe the arsDCAB genes.[7][8] ArsD and ArsR work together to regulate the ars operon.[9]

arsenic chaperone, ArsD, encoded by the arsRDABC operon of Escherichia coli. ArsD transfers trivalent metalloids to ArsA, the catalytic subunit of an As(III)/Sb(III) efflux pump. Interaction with ArsD increases the affinity of ArsA for arsenite, thus increasing its ATPase activity at lower concentrations of arsenite and enhancing the rate of arsenite extrusion. [10]


  1. ^ Carlin A, Shi W, Dey S, Rosen BP (February 1995). "The ars operon of Escherichia coli confers arsenical and antimonial resistance". J. Bacteriol. 177 (4): 981–6. PMC 176692. PMID 7860609. 
  2. ^ Liu J, Rosen BP (August 1997). "Ligand interactions of the ArsC arsenate reductase". J. Biol. Chem. 272 (34): 21084–9. doi:10.1074/jbc.272.34.21084. PMID 9261111. 
  3. ^ Rosen BP (1990). "The plasmid-encoded arsenical resistance pump: an anion-translocating ATPase.". Res Microbiol 141 (3): 336–41. doi:10.1016/0923-2508(90)90008-e. PMID 1704144. 
  4. ^ Martin P, DeMel S, Shi J, Gladysheva T, Gatti DL, Rosen BP, Edwards BF (November 2001). "Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme". Structure 9 (11): 1071–81. doi:10.1016/S0969-2126(01)00672-4. PMID 11709171. 
  5. ^ Zuber P (April 2004). "Spx-RNA polymerase interaction and global transcriptional control during oxidative stress". J. Bacteriol. 186 (7): 1911–8. doi:10.1128/jb.186.7.1911-1918.2004. PMC 374421. PMID 15028674. 
  6. ^ Li S, Rosen BP, Borges-Walmsley MI, Walmsley AR (July 2002). "Evidence for cooperativity between the four binding sites of dimeric ArsD, an As(III)-responsive transcriptional regulator". J. Biol. Chem. 277 (29): 25992–6002. doi:10.1074/jbc.M201619200. PMID 11980902. 
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This article incorporates text from the public domain Pfam and InterPro IPR006660

This article incorporates text from the public domain Pfam and InterPro IPR000802

This article incorporates text from the public domain Pfam and InterPro IPR010712

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Arsenical pump membrane protein Provide feedback

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This tab holds annotation information from the InterPro database.

InterPro entry IPR000802

Arsenic is a toxic metalloid whose trivalent and pentavalent ions inhibit a variety of biochemical processes. Operons that encode arsenic resistance have been found in multicopy plasmids from both Gram-positive and Gram-negative bacteria [PUBMED:7721697]. The resistance mechanism is encoded from a single operon, which houses an anion pump. The pump has two polypeptide components: a catalytic subunit (the ArsA protein), which functions as an oxyanion-stimulated ATPase; and an arsenite export component (the ArsB protein), which is associated with the inner membrane [PUBMED:1688427]. The ArsA and ArsB proteins are thought to form a membrane complex that functions as an anion-translocating ATPase.

The ArsB protein is distinguished by its overall hydrophobic character, in keeping with its role as a membrane-associated channel. Sequence analysis reveals the presence of 13 putative transmembrane (TM) regions.

Gene Ontology

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Domain organisation

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Pfam Clan

This family is a member of clan IT (CL0182), which has the following description:

This superfamily of secondary carriers specific for cationic and anionic compounds, has been termed the ion transporter (IT) superfamily [1].

The clan contains the following 19 members:

ABG_transport ArsB CitMHS CitMHS_2 DctM DcuA_DcuB DcuC DUF1646 DUF401 EXS GntP_permease Lactate_perm MatC_N Na_H_antiport_2 Na_H_antiport_3 Na_H_antiporter Na_sulph_symp NhaB SCFA_trans


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Seed source: IPR000802
Previous IDs: none
Type: Family
Author: Mian N, Bateman A
Number in seed: 2
Number in full: 11275
Average length of the domain: 385.50 aa
Average identity of full alignment: 52 %
Average coverage of the sequence by the domain: 97.24 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.2 22.2
Trusted cut-off 22.2 22.2
Noise cut-off 22.1 22.1
Model length: 423
Family (HMM) version: 11
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