Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5HRI4 (ARSC1_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 1
Alternative name(s):
Arsenate reductase 1
EC=1.20.4.-
Arsenical pump modifier 1
Low molecular weight protein-tyrosine-phosphatase 1
EC=3.1.3.48
Gene names
Name:arsC1
Ordered Locus Names:SERP0209
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length132 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. HAMAP-Rule MF_01624

Sequence similarities

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

Ontologies

Keywords
   Biological processArsenical resistance
   DomainRedox-active center
   Molecular functionHydrolase
Oxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
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 – 132132Protein ArsC 1 HAMAP-Rule MF_01624
PRO_0000162528

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
Q5HRI4 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 89634C648FBC115F

FASTA13214,658
        10         20         30         40         50         60 
MQKKTIYFIC TGNSCRSQMA EGFGKLILGD KWNVYSAGIE THGVNPHAIK AMKEVGIDIS 

        70         80         90        100        110        120 
HHTSDLINND ILIASDIVVT LCSDADANCP VLPKNVTKEH WGFDDPAGKD WSEFQRVRDE 

       130 
IKAAIETFAH RV 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW53573.1.
RefSeqYP_187805.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HRI4.
SMRQ5HRI4. Positions 1-131.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP0209.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW53573; AAW53573; SERP0209.
GeneID3242989.
KEGGser:SERP0209.
PATRIC19611307. VBIStaEpi130894_0200.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0394.
HOGENOMHOG000273093.
KOK03741.
OMASANEACP.
OrthoDBEOG6JDWJC.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-229-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. SSF52788. 1 hit.
TIGRFAMsTIGR02691. arsC_pI258_fam. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARSC1_STAEQ
AccessionPrimary (citable) accession number: Q5HRI4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 71 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