Summary: ArsC family
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This is the Wikipedia entry entitled "Ars operon". More...
Ars operon Edit Wikipedia article
| Anion-transporting ATPase | |||||||||
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| Identifiers | |||||||||
| Symbol | ArsA_ATPase | ||||||||
| Pfam | PF02374 | ||||||||
| Pfam clan | CL0023 | ||||||||
| SCOP | 1f48 | ||||||||
| SUPERFAMILY | 1f48 | ||||||||
| TCDB | 3.A.4 | ||||||||
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| ArsB | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | ArsB | ||||||||
| Pfam | PF02040 | ||||||||
| Pfam clan | CL0182 | ||||||||
| InterPro | IPR000802 | ||||||||
| TCDB | 3.A.4 | ||||||||
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| ArsC | |||||||||
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yffb (pa3664) protein |
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| Identifiers | |||||||||
| Symbol | ArsC | ||||||||
| Pfam | PF03960 | ||||||||
| Pfam clan | CL0172 | ||||||||
| InterPro | IPR006660 | ||||||||
| SCOP | 1i9d | ||||||||
| SUPERFAMILY | 1i9d | ||||||||
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| ArsD | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | ArsD | ||||||||
| Pfam | PF06953 | ||||||||
| Pfam clan | CL0172 | ||||||||
| InterPro | IPR010712 | ||||||||
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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]
Contents |
[edit] 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.
[edit] ArsC
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]
[edit] 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]
[edit] References
- ^ 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.
- ^ 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.
- ^ Rosen BP (1990). "The plasmid-encoded arsenical resistance pump: an anion-translocating ATPase.". Res Microbiol 141 (3): 336–41. PMID 1704144.
- ^ 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.
- ^ Zuber P (April 2004). "Spx-RNA polymerase interaction and global transcriptional control during oxidative stress". J. Bacteriol. 186 (7): 1911–8. PMC 374421. PMID 15028674.
- ^ 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.
- ^ http://www.springerimages.com/Images/RSS/1-10.1007_s00216-009-2785-x-0
- ^ http://www.ncbi.nlm.nih.gov/pubmed/9188467?dopt=Abstract
- ^ http://www.jbc.org/content/272/22/14257.long
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.
ArsC family Provide feedback
This family is related to glutaredoxins PF00462.
Internal database links
| SCOOP: | Y_phosphatase3C HSDR_N |
| Similarity to PfamA using HHSearch: | Glutaredoxin |
External database links
| PANDIT: | PF03960 |
| Pseudofam: | PF03960 |
| SCOP: | 1i9d |
| SYSTERS: | ArsC |
This tab holds annotation information from the InterPro database.
InterPro entry IPR006660
Several bacterial taxon have a chromosomal resistance system, encoded by the ars operon, for the detoxification of arsenate, arsenite, and antimonite [PUBMED:7860609]. 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 [PUBMED:9261111].
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 [PUBMED:15028674].
The arsC protein structure has been solved [PUBMED:11709171]. 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.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Thioredoxin (CL0172), which contains the following 45 members:
2Fe-2S_thioredx AhpC-TSA AhpC-TSA_2 ArsC ArsD Calsequestrin DIM1 DSBA DUF1525 DUF1687 DUF2703 DUF4174 DUF836 DUF899 DUF953 ERp29_N Glutaredoxin GSHPx GST_N GST_N_2 GST_N_3 HyaE KaiB MRP-S23 MRP-S25 OST3_OST6 Phosducin Redoxin SCO1-SenC SelP_N SH3BGR T4_deiodinase Thioredox_DsbH Thioredoxin Thioredoxin_2 Thioredoxin_3 Thioredoxin_4 Thioredoxin_5 Thioredoxin_6 Thioredoxin_7 Thioredoxin_8 Thioredoxin_9 Tom37 TraF YtfJ_HI0045Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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| Seed (36) |
Full (7591) |
Representative proteomes | NCBI (4303) |
Meta (1099) |
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| RP15 (315) |
RP35 (718) |
RP55 (1014) |
RP75 (1253) |
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| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
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| Seed (36) |
Full (7591) |
Representative proteomes | NCBI (4303) |
Meta (1099) |
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| RP15 (315) |
RP35 (718) |
RP55 (1014) |
RP75 (1253) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | COG1393 |
| Previous IDs: | none |
| Type: | Family |
| Author: | Bateman A |
| Number in seed: | 36 |
| Number in full: | 7591 |
| Average length of the domain: | 107.40 aa |
| Average identity of full alignment: | 26 % |
| Average coverage of the sequence by the domain: | 86.65 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 110 | ||||||||||||
| Family (HMM) version: | 10 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
RNA_pol_A_CTDStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ArsC domain has been found. There are 24 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence