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Literature summary for 7.3.2.7 extracted from

  • Wu, B.; Song, J.; Beitz, E.
    Novel channel enzyme fusion proteins confer arsenate resistance (2010), J. Biol. Chem., 285, 40081-40087.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.3.2.7

Cloned(Commentary)

Cloned (Comment) Organism
genes strop634 and strop1447, expression of enzyme mutants in Escherichia coli strain EPI300 with pCC1FOS-based fosmids Salinispora tropica

Protein Variants

Protein Variants Comment Organism
additional information construction of a truncated mutant by gene deletions disrupting strop634 and strop1447 in strain CNB-440, lack of Strop634 renders the single and double deletion strains highly sensitive to arsenate exposure, whereas in the absence of Strop1447, the cells unexpectedly display a normal resistance level, complementation of ACR2 deficient yeast strains by expression of Strop634, overview Salinispora tropica

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Salinispora tropica 16020
-

Organism

Organism UniProt Comment Textmining
Frankia alni
-
-
-
Mycobacterium tuberculosis
-
 gene Rv2643
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Mycobacterium tuberculosis H37Rv
-
 gene Rv2643
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Salinispora tropica
-
 genes strop634 and strop1447 encoding ACR2 and Ars2, respectively
-

Source Tissue

Source Tissue Comment Organism Textmining
mycelium
-
 Salinispora tropica
-

Subunits

Subunits Comment Organism
More the Strop634-Strop1447 protein interface is compatible permitting heterotetramer formation Salinispora tropica

Synonyms

Synonyms Comment Organism
Acr2
-
 Salinispora tropica
ACR2-ArsC
-
 Salinispora tropica
ACR3
-
 Mycobacterium tuberculosis
ACR3
-
 Frankia alni
ACR3-ArsC
-
 Mycobacterium tuberculosis
ACR3-ArsC
-
 Frankia alni
ACR3-ArsC fusion protein
-
 Mycobacterium tuberculosis
Rv2643
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
malfunction mutations rendered the aquaglyceroporin channel more polar resulting in lower glycerol permeability and enhanced arsenite selectivity Salinispora tropica
additional information the Strop634 channel domain has enhanced selectivity for arsenite and low glycerol permeability Salinispora tropica
physiological function the actinomycete from marine environment harbors a fusion protein consisting of an aquaglyceroporin-derived arsenite channel with a C-terminal arsenate reductase domain of phosphotyrosine-phosphatase origin, providing transposable, single gene-encoded arsenate resistance. The arsenate reductase domain couples to thioredoxin and can complement arsenate-sensitive yeast strains. A second isoform Strop1447 with a nonfunctional channel is coupled to the mycothiol/mycoredoxin system and may use the mycothiol/mycoredoxin cofactor pool. The channel-enzyme fusion protein, Strop634, confers arsenate resistance in Salinispora tropica Salinispora tropica
physiological function the arctinobacterium from soil harbors a fusion protein consisting of an aquaglyceroporin-derived arsenite channel with a C-terminal arsenate reductase domain of phosphotyrosine-phosphatase origin, providing transposable, single gene-encoded arsenate resistance Frankia alni
physiological function the bacterium harbors a fusion protein consisting of an aquaglyceroporin-derived arsenite channel with a C-terminal arsenate reductase domain of phosphotyrosine-phosphatase origin, providing transposable, single gene-encoded arsenate resistance. Strop634 and the ACR3-ArsC fusion protein Rv2643 from Mycobacterium tuberculosis are able to detoxify arsenate, whereas Strop1447 and two chimeras with Strop634 carrying either the Strop1447 channel or ArsC domain are not Mycobacterium tuberculosis