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Q540U1 (APHA_SALTM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Class B acid phosphatase
Short name=CBAP
EC=3.1.3.2
Gene names
Name:aphA
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

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. 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 Probable. Ref.1

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.1 Ref.2

Cofactor

Binds 1 magnesium ion per subunit. Ref.2

Subunit structure

Homotetramer. Ref.1 Ref.2

Subcellular location

Periplasm Probable Ref.1.

Sequence similarities

Belongs to the class B bacterial acid phosphatase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.15 mM for pNPP (in the presence of 1 mM MgCl2 at 37 degrees Celsius and pH 5.6) Ref.2

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Direct protein sequencing
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

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 Ref.1
Chain24 – 237214Class B acid phosphatase
PRO_0000414922

Regions

Region137 – 1382Substrate binding

Sites

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

Experimental info

Mutagenesis1771K → N: 40-fold reduction in phosphatase activity. 5.6-fold increase in KM for pNPP in presence of 1 mM MgCl(2). Ref.2
Mutagenesis1771K → R: 20-fold reduction in phosphatase activity. Nearly 2-fold increase in KM for pNPP in presence of 1 mM MgCl(2). Ref.2
Mutagenesis1961D → N: 6-fold reduction in phosphatase activity. 10000-fold decrease in affinity for Mg(2+). 18-fold increase in KM for pNPP in presence of 1 mM MgCl(2). KM is 0.79 mM for pNPP in the presence of 10 mM MgCl(2). Ref.2
Sequence conflict1181V → A in AAW22868. Ref.1

Secondary structure

1 ........................................ 237
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q540U1 [UniParc].

Last modified May 24, 2005. 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

[1]"Expression, purification, crystallization and preliminary X-ray diffraction studies of recombinant class B non-specific acid phosphatase of Salmonella typhimurium."
Makde R.D., Kumar V., Gupta G.D., Jasti J., Singh T.P., Mahajan S.K.
Acta Crystallogr. D 59:1849-1852(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-38 AND 40-46, FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, CRYSTALLIZATION.
Strain: MD6001.
[2]"Structural and mutational analyses reveal the functional role of active-site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein."
Makde R.D., Gupta G.D., Mahajan S.K., Kumar V.
Arch. Biochem. Biophys. 464:70-79(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-237 OF WILD-TYPE AND MUTANTS ARG/ASN-177 IN COMPLEXES WITH CAMP; PHOSPHATE AND MAGNESIUM IONS, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF LYS-177 AND ASP-196.
Strain: MD6001.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY125468 Genomic DNA. Translation: AAM95781.1.
AY841758 Genomic DNA. Translation: AAW22868.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z5GX-ray2.00A/B/C/D24-237[»]
1Z5UX-ray2.30A/B/C/D24-237[»]
1Z88X-ray2.10A/B/C/D24-237[»]
2AUTX-ray2.25A/B/C/D24-237[»]
ProteinModelPortalQ540U1.
SMRQ540U1. Positions 27-237.
ModBaseSearch...

Proteomic databases

PRIDEQ540U1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01672. AphA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAPHA_SALTM
AccessionPrimary (citable) accession number: Q540U1
Secondary accession number(s): Q5MB24
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: May 24, 2005
Last modified: April 3, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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