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P45947 (ARSC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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 (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
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. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 139139Protein ArsC HAMAP-Rule 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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D32216 Genomic DNA. Translation: BAA06970.1.
D84432 Genomic DNA. Translation: BAA12434.1.
AL009126 Genomic DNA. Translation: CAB14519.1.
PIRC69950.
RefSeqNP_390455.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JL3X-ray1.60A/B/C/D1-139[»]
1Z2DNMR-A1-139[»]
1Z2ENMR-A1-139[»]
2IPANMR-B1-139[»]
ProteinModelPortalP45947.
SMRP45947. Positions 3-139.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU25780.

Proteomic databases

PaxDbP45947.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14519; CAB14519; BSU25780.
GeneID937801.
KEGGbsu:BSU25780.
PATRIC18977000. VBIBacSub10457_2689.

Organism-specific databases

GenoListBSU25780. [Micado]

Phylogenomic databases

eggNOGCOG0394.
HOGENOMHOG000273093.
KOK03741.
OMAEMRIVIT.
OrthoDBEOG6JDWJC.
ProtClustDBPRK13530.

Enzyme and pathway databases

BioCycBSUB:BSU25780-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...

Other

EvolutionaryTraceP45947.

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: April 16, 2014
This is version 108 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

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