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P0A006 (ARSC_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein ArsC
Alternative name(s):
Arsenate reductase
EC=1.20.4.-
Arsenical pump modifier
Low molecular weight protein-tyrosine-phosphatase
EC=3.1.3.48
Gene names
Name:arsC
Encoded onPlasmid pI258 Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length131 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduces arsenate [As(V)] to arsenite [As(III)] and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Could switch between different functions in different circumstances. HAMAP-Rule MF_01624

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. HAMAP-Rule MF_01624

Arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O. HAMAP-Rule MF_01624

Enzyme regulation

Inhibited by arsenite (mixed inhibitor). HAMAP-Rule MF_01624

Subunit structure

Monomer.

Post-translational modification

Cys-89 performs a nucleophilic attack on a Cys-10-Cys-82 intermediate, forming another disulfide intermediate with Cys-82. HAMAP-Rule MF_01624

Miscellaneous

Cys-10 is essential for both reductase and phosphatase reactions.

Sequence similarities

Belongs to the low molecular weight phosphotyrosine protein phosphatase superfamily. ArsC family.

Biophysicochemical properties

Kinetic parameters:

Arsenate is the physiological substrate.

KM=146 mM for para-nitrophenyl phosphate (reduced form only) Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

KM=68 µM for arsenate

KM=0.8 µM for arsenate (below 1mM arsenate)

KM=2 mM for arsenate (above 1mM arsenate)

KM=13 mM for selenate

Vmax=200 nmol/min/mg enzyme (below 1 mM arsenate)

Vmax=450 nmol/min/mg enzyme (above 1 mM arsenate)

pH dependence:

Optimum pH is 8.

Mass spectrometry

Molecular mass is 14810.5 Da from positions 1 - 131. Determined by ESI. Ref.4

Molecular mass is 14812 Da from positions 1 - 131. Determined by ESI. Ref.6

Ontologies

Keywords
   Biological processArsenical resistance
   DomainRedox-active center
   Molecular functionHydrolase
Oxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
Plasmid
Gene Ontology (GO)
   Biological_processresponse to arsenic-containing substance

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionarsenate reductase (thioredoxin) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 131131Protein ArsC HAMAP-Rule MF_01624
PRO_0000162523

Sites

Active site101Nucleophile; for reductase activity and phosphatase activity
Active site821Nucleophile; for reductase activity
Active site891Nucleophile; for reductase activity

Amino acid modifications

Disulfide bond10 ↔ 82Redox-active; alternate HAMAP-Rule MF_01624
Disulfide bond82 ↔ 89Redox-active; alternate HAMAP-Rule MF_01624

Natural variations

Natural variant21D → T in strain: SW18, SW4, SW24 and SW1.
Natural variant24 – 3310GKEILGEGWN → AKQILAKDWD in strain: SW18.
Natural variant24 – 318GKEILGEG → AKQILADD in strain: SW24 and SW1.
Natural variant24 – 318GKEILGEG → AKQILAED in strain: SW4.
Natural variant561D → G in strain: SW18, SW4, SW24 and SW1.
Natural variant651D → N in strain: SW24 and SW1.
Natural variant70 – 767DILKQSD → NIIKNSN in strain: SW18, SW4, SW24 and SW1.
Natural variant871N → V in strain: SW18, SW4, SW24 and SW1.
Natural variant911I → S in strain: SW4, SW24 and SW1.
Natural variant911I → T in strain: SW18.
Natural variant941P → T in strain: SW18, SW4, SW24 and SW1.
Natural variant1101E → P in strain: SW18, SW4, SW24 and SW1.
Natural variant1231L → I in strain: SW4, SW24 and SW1.
Natural variant1231L → V in strain: SW18.
Natural variant1271K → N in strain: SW18, SW4, SW24 and SW1.
Natural variant1301L → S in strain: SW18, SW4, SW24 and SW1.

Experimental info

Mutagenesis101C → S: Loss of reductase and phosphatase activities. Loss of reductase and phosphatase activities; when associated with A-15. Ref.5
Mutagenesis151C → A: Decrease in substrate affinity of reductase. Substrate affinity of phosphatase identical to wild-type. Loss of reductase and phosphatase activities; when associated with S-10. Ref.5
Mutagenesis161R → K: Loss of reductase activity. Ref.8
Mutagenesis171S → A: 5-fold decrease in catalytic efficiency. Ref.8
Mutagenesis821C → S: Loss of reductase activity. Increase in substrate affinity of phosphatase. Ref.5
Mutagenesis891C → A: Loss of reductase activity. Ref.5 Ref.8
Mutagenesis891C → L: Decrease in substrate affinity of phosphatase. Leads to a reductase locked in the C-10/C-82 intermediate form. Ref.5 Ref.8
Mutagenesis1051D → A: 55-fold decrease in substrate affinity of reductase. Ref.8

Secondary structure

................... 131
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A006 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 03871148DC433A18

FASTA13114,813
        10         20         30         40         50         60 
MDKKTIYFIC TGNSCRSQMA EGWGKEILGE GWNVYSAGIE THGVNPKAIE AMKEVDIDIS 

        70         80         90        100        110        120 
NHTSDLIDND ILKQSDLVVT LCSDADNNCP ILPPNVKKEH WGFDDPAGKE WSEFQRVRDE 

       130 
IKLAIEKFKL R 

« Hide

References

[1]"Regulation and expression of the arsenic resistance operon from Staphylococcus aureus plasmid pI258."
Ji G., Silver S.
J. Bacteriol. 174:3684-3694(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of a collection of clinical Staphylococcus aureus wound isolates."
Tibor L., Cramton S.E., Goetz F., Hunt T.K.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SW1, SW18, SW24 and SW4.
[3]"Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258."
Ji G., Silver S.
Proc. Natl. Acad. Sci. U.S.A. 89:9474-9478(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Arsenate reductase of Staphylococcus aureus plasmid pI258."
Ji G., Garber E.A.E., Armes L.G., Chen C.-M., Fuchs J.A., Silver S.
Biochemistry 33:7294-7299(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
[5]"The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus."
Messens J., Hayburn G., Desmyter A., Laus G., Wyns L.
Biochemistry 38:16857-16865(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-10; CYS-15; CYS-82; CYS-89 AND 10-CYS--CYS-15, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"Kinetics and active site dynamics of Staphylococcus aureus arsenate reductase."
Messens J., Martins J.C., Brosens E., Van Belle K., Jacobs D.M., Willem R., Wyns L.
J. Biol. Inorg. Chem. 7:146-156(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, STRUCTURE BY NMR.
[7]"Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty."
Zegers I., Martins J.C., Willem R., Wyns L., Messens J.
Nat. Struct. Biol. 8:843-847(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF REDUCED AND OXIDIZED FORM OF MUTANT CYS-10--CYS-15, BIOPHYSICOCHEMICAL PROPERTIES.
[8]"All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade."
Messens J., Martins J.C., Van Belle K., Brosens E., Desmyter A., De Gieter M., Wieruszeski J.-M., Willem R., Wyns L., Zegers I.
Proc. Natl. Acad. Sci. U.S.A. 99:8506-8511(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF WILD-TYPE, MUTANT CYS-15 IN COMPLEX WITH ARSENITE AND CYS-89, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-16; SER-17; CYS-89 AND ASP-105, STRUCTURE BY NMR OF MUTANT CYS-82 AND CYS-89.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86824 Genomic DNA. Translation: AAA25638.1.
AY194061 Genomic DNA. Translation: AAP32334.1.
AY194062 Genomic DNA. Translation: AAP32338.1.
AY194064 Genomic DNA. Translation: AAP32346.1.
AY194065 Genomic DNA. Translation: AAP32350.1.
PIRA53641.
D41903.
RefSeqYP_001573918.1. NC_010077.1.
YP_001715971.1. NC_010419.1.
YP_006937217.1. NC_013292.1.
YP_006937607.1. NC_013319.1.
YP_006937727.1. NC_013322.1.
YP_006937753.1. NC_013323.1.
YP_006938161.1. NC_013333.1.
YP_006938435.1. NC_013340.1.
YP_006938641.1. NC_013347.1.
YP_006938712.1. NC_013349.1.
YP_006938775.1. NC_013352.1.
YP_006939395.1. NC_018965.1.
YP_006940871.1. NC_019009.1.
YP_536862.1. NC_007931.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JF8X-ray1.12A1-131[»]
1JFVX-ray2.00A1-131[»]
1LJLX-ray2.01A1-131[»]
1LJUX-ray1.40A1-131[»]
1LK0X-ray1.60A/B1-131[»]
1RXEX-ray1.70A1-131[»]
1RXIX-ray1.50A1-131[»]
2CD7X-ray1.50A1-131[»]
2FXIX-ray1.80A1-131[»]
ProteinModelPortalP0A006.
SMRP0A006. Positions 2-131.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13874340.
13874755.
13874878.
13874905.
13875324.
13875605.
13875818.
13875891.
13875956.
13876308.
13877846.
3978621.
5759819.
6155824.

Phylogenomic databases

ProtClustDBPRK13530.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-10862.
SABIO-RKP0A006.

Family and domain databases

HAMAPMF_01624. Arsenate_reduct.
InterProIPR014064. Arsenate_reductase_ArsC.
IPR023485. Ptyr_pPase_SF.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERPTHR11717. PTHR11717. 1 hit.
PfamPF01451. LMWPc. 1 hit.
[Graphical view]
SMARTSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMSSF52788. SSF52788. 1 hit.
TIGRFAMsTIGR02691. arsC_pI258_fam. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A006.

Entry information

Entry nameARSC_STAAU
AccessionPrimary (citable) accession number: P0A006
Secondary accession number(s): P30330 expand/collapse secondary AC list , Q6Y0M0, Q6Y0M4, Q6Y0N2, Q8GQH3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references