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P0A006

- ARSC_STAAU

UniProt

P0A006 - ARSC_STAAU

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Protein

Protein ArsC

Gene

arsC

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O.

Enzyme regulationi

Inhibited by arsenite (mixed inhibitor).

Kineticsi

Arsenate is the physiological substrate.

  1. KM=146 mM for para-nitrophenyl phosphate (reduced form only)5 Publications
  2. KM=68 µM for arsenate5 Publications
  3. KM=0.8 µM for arsenate (below 1mM arsenate)5 Publications
  4. KM=2 mM for arsenate (above 1mM arsenate)5 Publications
  5. KM=13 mM for selenate5 Publications

Vmax=200 nmol/min/mg enzyme (below 1 mM arsenate)5 Publications

Vmax=450 nmol/min/mg enzyme (above 1 mM arsenate)5 Publications

pH dependencei

Optimum pH is 8.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Nucleophile; for reductase activity and phosphatase activity
Active sitei82 – 821Nucleophile; for reductase activity
Active sitei89 – 891Nucleophile; for reductase activity

GO - Molecular functioni

  1. arsenate reductase (thioredoxin) activity Source: UniProtKB-HAMAP
  2. protein tyrosine phosphatase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. response to arsenic-containing substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Arsenical resistance

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10862.
SABIO-RKP0A006.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:arsC
Encoded oniPlasmid pI2587 Publications
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101C → S: Loss of reductase and phosphatase activities. Loss of reductase and phosphatase activities; when associated with A-15. 1 Publication
Mutagenesisi15 – 151C → 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. 1 Publication
Mutagenesisi16 – 161R → K: Loss of reductase activity. 1 Publication
Mutagenesisi17 – 171S → A: 5-fold decrease in catalytic efficiency. 1 Publication
Mutagenesisi82 – 821C → S: Loss of reductase activity. Increase in substrate affinity of phosphatase. 1 Publication
Mutagenesisi89 – 891C → A: Loss of reductase activity. 2 Publications
Mutagenesisi89 – 891C → L: Decrease in substrate affinity of phosphatase. Leads to a reductase locked in the C-10/C-82 intermediate form. 2 Publications
Mutagenesisi105 – 1051D → A: 55-fold decrease in substrate affinity of reductase. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 131131Protein ArsCPRO_0000162523Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi10 ↔ 82Redox-active; alternate
Disulfide bondi82 ↔ 89Redox-active; alternate

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
131
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1512Combined sources
Helixi16 – 2712Combined sources
Turni29 – 313Combined sources
Beta strandi32 – 409Combined sources
Helixi46 – 549Combined sources
Helixi69 – 746Combined sources
Beta strandi76 – 805Combined sources
Helixi83 – 886Combined sources
Beta strandi96 – 1005Combined sources
Helixi111 – 12919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0A006.
SMRiP0A006. Positions 2-131.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A006.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Family and domain databases

HAMAPiMF_01624. Arsenate_reduct.
InterProiIPR014064. Arsenate_reductase_ArsC.
IPR023485. Ptyr_pPase_SF.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF18. PTHR11717:SF18. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.
TIGRFAMsiTIGR02691. arsC_pI258_fam. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A006-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDKKTIYFIC TGNSCRSQMA EGWGKEILGE GWNVYSAGIE THGVNPKAIE
60 70 80 90 100
AMKEVDIDIS NHTSDLIDND ILKQSDLVVT LCSDADNNCP ILPPNVKKEH
110 120 130
WGFDDPAGKE WSEFQRVRDE IKLAIEKFKL R
Length:131
Mass (Da):14,813
Last modified:February 15, 2005 - v1
Checksum:i03871148DC433A18
GO

Mass spectrometryi

Molecular mass is 14810.5 Da from positions 1 - 131. Determined by ESI. 1 Publication
Molecular mass is 14812 Da from positions 1 - 131. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21D → T in strain: SW18, SW4, SW24 and SW1.
Natural varianti24 – 3310GKEILGEGWN → AKQILAKDWD in strain: SW18.
Natural varianti24 – 318GKEILGEG → AKQILADD in strain: SW24 and SW1.
Natural varianti24 – 318GKEILGEG → AKQILAED in strain: SW4.
Natural varianti56 – 561D → G in strain: SW18, SW4, SW24 and SW1.
Natural varianti65 – 651D → N in strain: SW24 and SW1.
Natural varianti70 – 767DILKQSD → NIIKNSN in strain: SW18, SW4, SW24 and SW1.
Natural varianti87 – 871N → V in strain: SW18, SW4, SW24 and SW1.
Natural varianti91 – 911I → S in strain: SW4, SW24 and SW1.
Natural varianti91 – 911I → T in strain: SW18.
Natural varianti94 – 941P → T in strain: SW18, SW4, SW24 and SW1.
Natural varianti110 – 1101E → P in strain: SW18, SW4, SW24 and SW1.
Natural varianti123 – 1231L → I in strain: SW4, SW24 and SW1.
Natural varianti123 – 1231L → V in strain: SW18.
Natural varianti127 – 1271K → N in strain: SW18, SW4, SW24 and SW1.
Natural varianti130 – 1301L → S in strain: SW18, SW4, SW24 and SW1.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA53641.
D41903.
RefSeqiWP_000358995.1. NC_019009.1.
YP_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.

Genome annotation databases

GeneIDi13874340.
13874755.
13874878.
13874905.
13875324.
13875605.
13875818.
13875891.
13875956.
13876308.
13877846.
3978621.
5759819.
6155824.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi A53641.
D41903.
RefSeqi WP_000358995.1. NC_019009.1.
YP_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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JF8 X-ray 1.12 A 1-131 [» ]
1JFV X-ray 2.00 A 1-131 [» ]
1LJL X-ray 2.01 A 1-131 [» ]
1LJU X-ray 1.40 A 1-131 [» ]
1LK0 X-ray 1.60 A/B 1-131 [» ]
1RXE X-ray 1.70 A 1-131 [» ]
1RXI X-ray 1.50 A 1-131 [» ]
2CD7 X-ray 1.50 A 1-131 [» ]
2FXI X-ray 1.80 A 1-131 [» ]
ProteinModelPortali P0A006.
SMRi P0A006. Positions 2-131.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 13874340.
13874755.
13874878.
13874905.
13875324.
13875605.
13875818.
13875891.
13875956.
13876308.
13877846.
3978621.
5759819.
6155824.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-10862.
SABIO-RK P0A006.

Miscellaneous databases

EvolutionaryTracei P0A006.

Family and domain databases

HAMAPi MF_01624. Arsenate_reduct.
InterProi IPR014064. Arsenate_reductase_ArsC.
IPR023485. Ptyr_pPase_SF.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view ]
PANTHERi PTHR11717:SF18. PTHR11717:SF18. 1 hit.
Pfami PF01451. LMWPc. 1 hit.
[Graphical view ]
SMARTi SM00226. LMWPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52788. SSF52788. 1 hit.
TIGRFAMsi TIGR02691. arsC_pI258_fam. 1 hit.
ProtoNeti Search...

Publicationsi

  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].
    Plasmid: pI258
  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.
    Plasmid: pI258
  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.
    Plasmid: pI258
  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.
    Plasmid: pI258
  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.
    Plasmid: pI258
  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.
    Plasmid: pI258
  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.
    Plasmid: pI258

Entry informationi

Entry nameiARSC_STAAU
AccessioniPrimary (citable) accession number: P0A006
Secondary accession number(s): P30330
, Q6Y0M0, Q6Y0M4, Q6Y0N2, Q8GQH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: November 26, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3