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P58683 (APHA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Class B acid phosphatase

Short name=CBAP
EC=3.1.3.2
Alternative name(s):
Non-specific acid phosphatase II
Gene names
Name:aphA
Ordered Locus Names:STM4249
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dephosphorylates several organic phosphate monoesters such as 3'-UMP, 5'-UMP and pNPP. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds such as the 2'-, 3-, or 5'-hydroxyls of nucleosides and nucleotides. Also displays significant phosphomutase activity since it is able to catalyze the transfer of the phosphate group of 3'-AMP from the 3'-position both to the 2'- and 5'-positions. One of the physiological functions of the phosphohydrolytic activity of the enzyme is believed to be the scavenging of organic phosphate esters that otherwise cannot pass the cytoplasmic membrane. Ref.2 Ref.3

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.2 Ref.3

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Enzyme regulation

Nucleosides, and particularly 2'-deoxyribonucleosides, are potent inhibitors of the phosphatase activity. The phosphatase activity is also inhibited by inorganic phosphate and EDTA in vitro. Ref.2 Ref.3

Subunit structure

Homotetramer. Ref.3

Subcellular location

Periplasm Ref.2.

Disruption phenotype

Cells lacking this gene show a severely decreased growth rate on 5'-UMP as pyrimidine source. Ref.2

Sequence similarities

Belongs to the class B bacterial acid phosphatase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.30 mM for 5'-UMP (at 37 degrees Celsius and pH 6.5) Ref.2

pH dependence:

Optimum pH is 5.0-5.5 and 6.5 for the phosphatase activity with 3'-UMP and 5'-UMP as substrate, respectively.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference 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: UniProtKB-EC

metal 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_0000024009

Regions

Region137 – 1382Substrate binding By similarity

Sites

Active site691Nucleophile By similarity
Active site711Proton donor By similarity
Metal binding691Magnesium By similarity
Metal binding711Magnesium; via carbonyl oxygen By similarity
Metal binding1921Magnesium By similarity
Binding site1771Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P58683 [UniParc].

Last modified January 31, 2002. Version 1.
Checksum: 386E11DC84C16269

FASTA23726,315
        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 KPEQNTKVQW 

       190        200        210        220        230 
LQEKNMRIFY GDSDNDITAA RDCGIRGIRI LRAANSTYKP LPQAGAFGEE VIVNSEY 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"Periplasmic phosphatases in Salmonella typhimurium LT2. A biochemical, physiological, and partial genetic analysis of three nucleoside monophosphate dephosphorylating enzymes."
Uerkvitz W., Beck C.F.
J. Biol. Chem. 256:382-389(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
Strain: LT2.
[3]"Periplasmic nonspecific acid phosphatase II from Salmonella typhimurium LT2. Crystallization, detergent reactivation, and phosphotransferase activity."
Uerkvitz W.
J. Biol. Chem. 263:15823-15830(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A PHOSPHOTRANSFERASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, CRYSTALLIZATION.
Strain: LT2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL23073.1.
RefSeqNP_463114.1. NC_003197.1.

3D structure databases

ProteinModelPortalP58683.
SMRP58683. Positions 27-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM4249.

Proteomic databases

PaxDbP58683.
PRIDEP58683.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL23073; AAL23073; STM4249.
GeneID1255775.
KEGGstm:STM4249.
PATRIC32387403. VBISalEnt20916_4469.

Phylogenomic databases

eggNOGCOG3700.
HOGENOMHOG000270623.
KOK03788.
OMAPEFWEKM.
OrthoDBEOG6HTNVZ.
PhylomeDBP58683.

Enzyme and pathway databases

BioCycSENT99287:GCTI-4280-MONOMER.
SABIO-RKP58683.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR005519. Acid_phosphat_B.
IPR023214. HAD-like_dom.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view]
PfamPF03767. Acid_phosphat_B. 1 hit.
[Graphical view]
PIRSFPIRSF017818. Acid_Ptase_B. 1 hit.
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01672. AphA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP58683.

Entry information

Entry nameAPHA_SALTY
AccessionPrimary (citable) accession number: P58683
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: July 9, 2014
This is version 86 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