Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein ArsC 2

Gene

arsC2

Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei10Nucleophile; for reductase activity and phosphatase activityUniRule annotation1
Active sitei82Nucleophile; for reductase activityUniRule annotation1
Active sitei89Nucleophile; for reductase activityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Arsenical resistance

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ArsC 2UniRule annotation
Alternative name(s):
Arsenate reductase 2UniRule annotation (EC:1.20.4.-UniRule annotation)
Arsenical pump modifier 2UniRule annotation
Low molecular weight protein-tyrosine-phosphatase 2UniRule annotation (EC:3.1.3.48UniRule annotation)
Gene namesi
Name:arsC2UniRule annotation
Ordered Locus Names:SH0108
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000543 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001625311 – 131Protein ArsC 2Add BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi10 ↔ 82Redox-active; alternateUniRule annotation
Disulfide bondi82 ↔ 89Redox-active; alternateUniRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi279808.SH0108.

Structurei

3D structure databases

ProteinModelPortaliQ4LAA8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4108UXE. Bacteria.
COG0394. LUCA.
HOGENOMiHOG000273093.
KOiK03741.
OMAiEMRIVIT.
OrthoDBiPOG091H07DS.

Family and domain databases

CDDicd00115. LMWPc. 1 hit.
HAMAPiMF_01624. Arsenate_reduct. 1 hit.
InterProiIPR014064. Arsenate_reductase_ArsC.
IPR023485. Ptyr_pPase_SF.
[Graphical view]
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.

Q4LAA8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKKTIYFIC TGNSCRSQMA EGWGKKILGD EWQVYSGGIE AHGVNPKAIE
60 70 80 90 100
AMKEVGIDIS NHTSNLIDKN ILNQSDLVVT LCSDADNNCP ILPPNVKKEH
110 120 130
WGFDDPAGKP WSEFQRVRDE IKTAIESFKT R
Length:131
Mass (Da):14,683
Last modified:August 2, 2005 - v1
Checksum:i4049813AF5BDB6F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE03417.1.
RefSeqiWP_011274439.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE03417; BAE03417; SH0108.
GeneIDi24246174.
KEGGisha:SH0108.
PATRICi19616253. VBIStaHae67511_0104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE03417.1.
RefSeqiWP_011274439.1. NC_007168.1.

3D structure databases

ProteinModelPortaliQ4LAA8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279808.SH0108.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE03417; BAE03417; SH0108.
GeneIDi24246174.
KEGGisha:SH0108.
PATRICi19616253. VBIStaHae67511_0104.

Phylogenomic databases

eggNOGiENOG4108UXE. Bacteria.
COG0394. LUCA.
HOGENOMiHOG000273093.
KOiK03741.
OMAiEMRIVIT.
OrthoDBiPOG091H07DS.

Family and domain databases

CDDicd00115. LMWPc. 1 hit.
HAMAPiMF_01624. Arsenate_reduct. 1 hit.
InterProiIPR014064. Arsenate_reductase_ArsC.
IPR023485. Ptyr_pPase_SF.
[Graphical view]
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.
TIGRFAMsiTIGR02691. arsC_pI258_fam. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiARSC2_STAHJ
AccessioniPrimary (citable) accession number: Q4LAA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: August 2, 2005
Last modified: November 2, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.