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Reviewed, UniProtKB/Swiss-Prot O08430 (APHA_SALTI)

Last modified February 9, 2010. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    Class B acid phosphatase
    EC=3.1.3.2
Gene names
Name: aphA
Synonyms: napA
Ordered Locus Names: STY4445, t4155
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Dephosphorylates several organic phosphomonoesters and catalyzes the transfer of low-energy phosphate groups from phosphomonoesters to hydroxyl groups of various organic compounds. Might function as a broad spectrum dephosphorylating enzyme able to scavenge both 3'- and 5'-nucleotides and also additional organic phosphomonoesters By similarity.

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

Periplasm Potential.

Sequence similarities

Belongs to the class B bacterial acid phosphatase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentouter membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular functionacid phosphatase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 237214Class B acid phosphatase
PRO_0000024008

Sites

Metal binding691Magnesium By similarity
Metal binding711Magnesium; via carbonyl oxygen By similarity
Metal binding1921Magnesium By similarity

Experimental info

Sequence conflict71Missing in CAB40974. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08430-1 [UniParc].

Last modified December 5, 2001. Version 2.
Checksum: 3B0D71DFE7A16269

FASTA23726,243
        10         20         30         40         50         60 
MKKITLALSA VCLLFTLNHS ANALVSSPST LNPGTNVAKL AEQAPVHWVS VAQIENSLTG 

        70         80         90        100        110        120 
RPPMAVGFDI DDTVLFSSPG FWRGKKTYSP DSDDYLKNPA FWEKMNNGWD EFSIPKEVAR 

       130        140        150        160        170        180 
QLIDMHVRRG DSIYFVTGRS QTKTETVSKT LADNFHIPAA NMNPVIFAGD KPGQNTKVQW 

       190        200        210        220        230 
LQEKNMRIFY GDSDNDITAA RDCGIRGIRI LRAANSTYKP LPQAGAFGEE VIVNSEY 

« Hide

References

« Hide 'large scale' references
[1]"Genetic rearrangements in the tyrB-uvrA region of the enterobacterial chromosome: a potential cause for different class B acid phosphatase regulation in Salmonella enterica and Escherichia coli."
Rossolini G.M., Bonci A., Schippa S., Berlutti F., Thaller M.C.
FEMS Microbiol. Lett. 181:17-23(1999) [PubMed: 10564784] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: STY4.
[2]"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. expand/collapse author list , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:848-852(2001) [PubMed: 11677608] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.
[3]"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ237788 Genomic DNA. Translation: CAB40974.1.
AL627282 Genomic DNA. Translation: CAD09233.1.
AE014613 Genomic DNA. Translation: AAO71619.1.
RefSeqNP_458547.1.
NP_807759.1.

3D structure databases

SMRO08430. Positions 27-237.
ModBaseSearch...

Genome annotation databases

GeneID1069720.
1250662.
GenomeReviewsGene locus t4155 in contig AE014613_GR.
KEGGstt:t4155.
sty:STY4445.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG698065.
OMAGQNTKTQ.

Enzyme and pathway databases

BioCycSENT209261:T4155-MONOMER.
SENT220341:STY4445-MONOMER.
BRENDA3.1.3.2. 3716.

Family and domain databases

InterProIPR005519. Acid_phosphat_B.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view]
PfamPF03767. Acid_phosphat_B. 1 hit.
[Graphical view]
PIRSFPIRSF017818. Acid_Ptase_B. 1 hit.
TIGRFAMsTIGR01672. AphA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAPHA_SALTI
AccessionPrimary (citable) accession number: O08430
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 5, 2001
Last modified: February 9, 2010
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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