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Q4LAA8 (ARSC2_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein ArsC 2
Alternative name(s):
Arsenate reductase 2
EC=1.20.4.-
Arsenical pump modifier 2
Low molecular weight protein-tyrosine-phosphatase 2
EC=3.1.3.48
Gene names
Name:arsC2
Ordered Locus Names:SH0108
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length131 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. 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

Subunit structure

Monomer By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 131131Protein ArsC 2 HAMAP-Rule MF_01624
PRO_0000162531

Sites

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

Amino acid modifications

Disulfide bond10 ↔ 82Redox-active; alternate By similarity
Disulfide bond82 ↔ 89Redox-active; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4LAA8 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 4049813AF5BDB6F7

FASTA13114,683
        10         20         30         40         50         60 
MDKKTIYFIC TGNSCRSQMA EGWGKKILGD EWQVYSGGIE AHGVNPKAIE AMKEVGIDIS 

        70         80         90        100        110        120 
NHTSNLIDKN ILNQSDLVVT LCSDADNNCP ILPPNVKKEH WGFDDPAGKP WSEFQRVRDE 

       130 
IKTAIESFKT R 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC1435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE03417.1.
RefSeqYP_252023.1. NC_007168.1.

3D structure databases

ProteinModelPortalQ4LAA8.
SMRQ4LAA8. Positions 2-131.
ModBaseSearch...

Protein-protein interaction databases

STRING279808.SH0108.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE03417; BAE03417; SH0108.
GeneID3482396.
KEGGsha:SH0108.
PATRIC19616253. VBIStaHae67511_0104.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0394.
HOGENOMHOG000273093.
KOK03741.
OMAEMRIVIT.
ProtClustDBPRK13530.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-110-MONOMER.

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. Tyr_Pase_low_mol_wt. 1 hit.
TIGRFAMsTIGR02691. arsC_pI258_fam. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARSC2_STAHJ
AccessionPrimary (citable) accession number: Q4LAA8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: August 2, 2005
Last modified: May 1, 2013
This is version 61 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