Reviewed,
UniProtKB/Swiss-Prot P45947 (ARSC_BACSU)
Last modified
June 16, 2009.
Version 73.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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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 |
| ||||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 139 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Arsenical resistance |
| Domain | Redox-active center |
| Molecular function | Hydrolase Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid dephosphorylationInferred from electronic annotation. Source: InterPro response to arsenicInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | arsenate reductase (thioredoxin) activity Inferred from electronic annotation. Source: HAMAP protein tyrosine phosphatase activityInferred 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 – 139 | 139 | Protein arsC HAMAP MF_01624 | PRO_0000162520 | ||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||
| Active site | 10 | 1 | Nucleophile; for reductase activity and phosphatase activity By similarity | |||||||||||||||||||||||||
| Active site | 82 | 1 | Nucleophile; for reductase activity By similarity | |||||||||||||||||||||||||
| Active site | 89 | 1 | Nucleophile; for reductase activity By similarity | |||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||
| Disulfide bond | 10 ↔ 82 | Redox-active; alternate By similarity | ||||||||||||||||||||||||||
| Disulfide bond | 82 ↔ 89 | Redox-active; alternate By similarity | ||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||
| Beta strand | 4 – 15 | 12 | ||||||||||||||||||||||||||
| Helix | 16 – 27 | 12 | ||||||||||||||||||||||||||
| Beta strand | 32 – 40 | 9 | ||||||||||||||||||||||||||
| Helix | 46 – 54 | 9 | ||||||||||||||||||||||||||
| Helix | 69 – 72 | 4 | ||||||||||||||||||||||||||
| Beta strand | 76 – 80 | 5 | ||||||||||||||||||||||||||
| Helix | 83 – 88 | 6 | ||||||||||||||||||||||||||
| Beta strand | 96 – 100 | 5 | ||||||||||||||||||||||||||
| Helix | 106 – 108 | 3 | ||||||||||||||||||||||||||
| Helix | 113 – 137 | 25 | ||||||||||||||||||||||||||
Sequences
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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. 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. | |||||||||||||||||||||||||||||||
| PIR | C69950. | ||||||||||||||||||||||||||||||
| RefSeq | NP_390455.1. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| GeneID | 937801. | ||||||||||||||||||||||||||||||
| GenomeReviews | Gene locus BSU25780 in contig AL009126_GR. | ||||||||||||||||||||||||||||||
| KEGG | bsu:BSU25780. | ||||||||||||||||||||||||||||||
| NMPDR | fig|224308.1.peg.2580. | ||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||
| SubtiList | BG11304. arsC. [Micado] | ||||||||||||||||||||||||||||||
| CMR | Search... | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| HOGENOM | P45947. | ||||||||||||||||||||||||||||||
| OMA | P45947. EMRIVIT. | ||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||
| BioCyc | BSUB224308:BSU2573-MON. | ||||||||||||||||||||||||||||||
| BRENDA | 3.1.3.48. 150. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| HAMAP | MF_01624. [Tree] | ||||||||||||||||||||||||||||||
| InterPro | IPR014064. Arsenate_reductase_StaphA. IPR017867. Tyr_phospatase_low_mol_wt. [Graphical view] | ||||||||||||||||||||||||||||||
| PANTHER | PTHR11717. Low_mwt_PTPase. 1 hit. | ||||||||||||||||||||||||||||||
| Pfam | PF01451. LMWPc. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| SMART | SM00226. LMWPc. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| TIGRFAMs | TIGR02691. arsC_pI258_fam. 1 hit. | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | ARSC_BACSU | ||||||||
| Accession | Primary (citable) accession number: P45947 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (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 |

Clusters with


