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Reviewed, UniProtKB/Swiss-Prot P45947 (ARSC_BACSU)

Last modified June 16, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
Synonyms: yqcM
Ordered Locus Names: BSU25780
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. HAMAP MF_01624

Arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O. HAMAP 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 – 139139Protein arsC HAMAP MF_01624
PRO_0000162520

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

Secondary structure

.................... 139
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45947-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 880EE1C77D1FE130

FASTA13915,595
        10         20         30         40         50         60 
MENKIIYFLC TGNSCRSQMA EGWAKQYLGD EWKVYSAGIE AHGLNPNAVK AMKEVGIDIS 

        70         80         90        100        110        120 
NQTSDIIDSD ILNNADLVVT LCGDAADKCP MTPPHVKREH WGFDDPARAQ GTEEEKWAFF 

       130 
QRVRDEIGNR LKEFAETGK 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of a skin element excised by DNA rearrangement during sporulation in Bacillus subtilis."
Takemaru K., Mizuno M., Sato T., Takeuchi M., Kobayashi Y.
Microbiology 141:323-327(1995) [PubMed: 7704261] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[2]"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
Microbiology 142:3103-3111(1996) [PubMed: 8969508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Analysis of a Bacillus subtilis genome fragment using a co-operative computer system prototype."
Medigue C., Moszer I., Viari A., Danchin A.
Gene 165:GC37-GC51(1995) [PubMed: 7489895] [Abstract]
Cited for: IDENTIFICATION.
[5]"The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite."
Sato T., Kobayashi Y.
J. Bacteriol. 180:1655-1661(1998) [PubMed: 9537360] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

D32216 Genomic DNA. Translation: BAA06970.1.
D84432 Genomic DNA. Translation: BAA12434.1.
AL009126 Genomic DNA. Translation: CAB14519.1.
PIRC69950.
RefSeqNP_390455.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JL3X-ray1.60A/B/C/D1-139[»]
1Z2DNMR-A1-139[»]
1Z2ENMR-A1-139[»]
2IPANMR-B1-139[»]
ModBaseSearch...

Genome annotation databases

GeneID937801.
GenomeReviewsGene locus BSU25780 in contig AL009126_GR.
KEGGbsu:BSU25780.
NMPDRfig|224308.1.peg.2580.

Organism-specific databases

SubtiListBG11304. arsC. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP45947.
OMAP45947. EMRIVIT.

Enzyme and pathway databases

BioCycBSUB224308:BSU2573-MON.
BRENDA3.1.3.48. 150.

Family and domain databases

HAMAPMF_01624.
[Tree]
InterProIPR014064. Arsenate_reductase_StaphA.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERPTHR11717. Low_mwt_PTPase. 1 hit.
PfamPF01451. LMWPc. 1 hit.
[Graphical view]
SMARTSM00226. LMWPc. 1 hit.
[Graphical view]
TIGRFAMsTIGR02691. arsC_pI258_fam. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARSC_BACSU
AccessionPrimary (citable) accession number: P45947
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents