Q6HGP0 (ARSC_BACHK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	arsC
Ordered Locus Names:	BT9727_2963

Organism

Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]

Taxonomic identifier

281309 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › Bacillus thuringiensis › Bacillus thuringiensis subsp. konkukian

Protein attributes

Sequence length	134 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Arsenical resistance
Domain	Redox-active center
Molecular function	Hydrolase Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC response to arsenic-containing substance Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	arsenate reductase (thioredoxin) activity Inferred from electronic annotation. Source: HAMAP protein tyrosine phosphatase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 134	134	Protein ArsC HAMAP-Rule MF_01624		PRO_0000162521
Sites
	Active site	11	1	Nucleophile; for reductase activity and phosphatase activity By similarity
	Active site	83	1	Nucleophile; for reductase activity By similarity
	Active site	90	1	Nucleophile; for reductase activity By similarity
Amino acid modifications
	Disulfide bond	11 ↔ 83		Redox-active; alternate By similarity
	Disulfide bond	83 ↔ 90		Redox-active; alternate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6HGP0 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: D3ADE8FC18C608A8	FASTA	134	15,019
	10 20 30 40 50 60 MENKKTIYFL CTGNSCRSQM AEAWGKQYLG DKWNVYSAGI EAHGVNPNAI KAMNEVNIDI 70 80 90 100 110 120 TNQTSDIIDA NILNRADLVV TLCSHADSVC PSTPPHVNRV HWGFDDPAGK EWSEFQRVRD 130 EIGERIKCFS ETGE

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT60271.1.
RefSeq	YP_037286.1. NC_005957.1.
3D structure databases
ProteinModelPortal	Q6HGP0.
SMR	Q6HGP0. Positions 1-134.
ModBase	Search...
Protein-protein interaction databases
STRING	281309.BT9727_2963.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT60271; AAT60271; BT9727_2963.
GeneID	2853620.
KEGG	btk:BT9727_2963.
PATRIC	18986856. VBIBacThu119411_3154.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0394.
HOGENOM	HOG000273093.
KO	K03741.
OMA	QTSDMID.
ProtClustDB	PRK13530.
Enzyme and pathway databases
BioCyc	BTHU281309:GJID-3040-MONOMER.
Family and domain databases
HAMAP	MF_01624. Arsenate_reduct.
InterPro	IPR014064. Arsenate_reductase_ArsC. IPR023485. Ptyr_pPase_SF. IPR017867. Tyr_phospatase_low_mol_wt. [Graphical view]
PANTHER	PTHR11717. PTHR11717. 1 hit.
Pfam	PF01451. LMWPc. 1 hit. [Graphical view]
SMART	SM00226. LMWPc. 1 hit. [Graphical view]
SUPFAM	SSF52788. Tyr_Pase_low_mol_wt. 1 hit.
TIGRFAMs	TIGR02691. arsC_pI258_fam. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARSC_BACHK

Accession

Primary (citable) accession number: Q6HGP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program