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P07102 (PPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 129. 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:
Periplasmic AppA protein

Including the following 2 domains:

  1. Phosphoanhydride phosphohydrolase
    EC=3.1.3.2
    Alternative name(s):
    pH 2.5 acid phosphatase
    Short name=AP
  2. 4-phytase
    EC=3.1.3.26
Gene names
Name:appA
Ordered Locus Names:b0980, JW0963
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate.

Subunit structure

Monomer.

Subcellular location

Periplasm.

Induction

In addition to cAMP-mediated control, this enzyme is induced when bacterial cultures reach stationary phase; its synthesis is triggered by phosphate starvation or a shift from aerobic to anaerobic conditions.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.1 Ref.7 Ref.8
Chain23 – 432410Periplasmic AppA protein
PRO_0000023947

Regions

Region42 – 465Substrate binding
Region325 – 3273Substrate binding

Sites

Active site391Nucleophile
Active site3261Proton donor
Binding site381Substrate
Binding site1141Substrate
Binding site2891Substrate

Amino acid modifications

Disulfide bond99 ↔ 130
Disulfide bond155 ↔ 430
Disulfide bond200 ↔ 210
Disulfide bond404 ↔ 413

Experimental info

Sequence conflict51 – 6616MQDVT…WPVKL → NAGCHPRRMANLAGKT in CAA29031. Ref.5
Sequence conflict75 – 762EL → DV in CAA29031. Ref.5
Sequence conflict1121D → S in CAA29031. Ref.5

Secondary structure

....................................................................... 432
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07102 [UniParc].

Last modified August 1, 1991. Version 2.
Checksum: 6510C6C579177F11

FASTA43247,057
        10         20         30         40         50         60 
MKAILIPFLS LLIPLTPQSA FAQSEPELKL ESVVIVSRHG VRAPTKATQL MQDVTPDAWP 

        70         80         90        100        110        120 
TWPVKLGWLT PRGGELIAYL GHYQRQRLVA DGLLAKKGCP QSGQVAIIAD VDERTRKTGE 

       130        140        150        160        170        180 
AFAAGLAPDC AITVHTQADT SSPDPLFNPL KTGVCQLDNA NVTDAILSRA GGSIADFTGH 

       190        200        210        220        230        240 
RQTAFRELER VLNFPQSNLC LKREKQDESC SLTQALPSEL KVSADNVSLT GAVSLASMLT 

       250        260        270        280        290        300 
EIFLLQQAQG MPEPGWGRIT DSHQWNTLLS LHNAQFYLLQ RTPEVARSRA TPLLDLIKTA 

       310        320        330        340        350        360 
LTPHPPQKQA YGVTLPTSVL FIAGHDTNLA NLGGALELNW TLPGQPDNTP PGGELVFERW 

       370        380        390        400        410        420 
RRLSDNSQWI QVSLVFQTLQ QMRDKTPLSL NTPPGEVKLT LAGCEERNAQ GMCSLAGFTQ 

       430 
IVNEARIPAC SL 

« Hide

References

« Hide 'large scale' references
[1]"The complete nucleotide sequence of the Escherichia coli gene appA reveals significant homology between pH 2.5 acid phosphatase and glucose-1-phosphatase."
Dassa J., Marck C., Boquet P.L.
J. Bacteriol. 172:5497-5500(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-29.
Strain: K12.
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The structure of the promoter and amino terminal region of the pH 2.5 acid phosphatase structural gene (appA) of E. coli: a negative control of transcription mediated by cyclic AMP."
Touati E., Danchin A.
Biochimie 69:215-221(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
[6]"A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA)."
Dassa J., Fsihi H., Marck C., Dion M., Kieffer-Bontemps M., Boquet P.L.
Mol. Gen. Genet. 229:341-352(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
Strain: K12.
[7]"Characterization of a phytase from Escherichia coli."
Greiner R., Jany K.-D.
Biol. Chem. Hoppe-Seyler 372:664-665(1991)
Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 23-34.
[8]"Purification and characterization of two phytases from Escherichia coli."
Greiner R., Konietzny U., Jany K.-D.
Arch. Biochem. Biophys. 303:107-113(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 23-35.
[9]"Characterization and overproduction of the Escherichia coli appA encoded bifunctional enzyme that exhibits both phytase and acid phosphatase activities."
Golovan S., Wang G., Zhang J., Forsberg C.W.
Can. J. Microbiol. 46:59-71(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[10]"Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase."
Ostanin K., Harms E.H., Stevis P.E., Kuciel R., Zhou M.-M., van Etten R.L.
J. Biol. Chem. 267:22830-22836(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[11]"Crystal structures of Escherichia coli phytase and its complex with phytate."
Lim D., Golovan S., Forsberg C.W., Jia Z.
Nat. Struct. Biol. 7:108-113(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH INOSITOL HEXAKISPHOSPHATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58708 Genomic DNA. Translation: AAA72086.1.
U00096 Genomic DNA. Translation: AAC74065.1.
AP009048 Genomic DNA. Translation: BAA35745.1.
X05471 Genomic DNA. Translation: CAA29031.1.
S63811 Genomic DNA. Translation: AAB20286.1.
PIRB36733.
RefSeqNP_415500.1. NC_000913.3.
YP_489251.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DKLX-ray2.30A/B23-432[»]
1DKMX-ray2.25A23-432[»]
1DKNX-ray2.40A23-432[»]
1DKOX-ray2.38A23-432[»]
1DKPX-ray2.28A23-432[»]
1DKQX-ray2.05A23-432[»]
ProteinModelPortalP07102.
SMRP07102. Positions 23-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP07102. 3 interactions.
STRING511145.b0980.

2D gel databases

SWISS-2DPAGEP07102.

Proteomic databases

PaxDbP07102.
PRIDEP07102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74065; AAC74065; b0980.
BAA35745; BAA35745; BAA35745.
GeneID12930360.
946206.
KEGGecj:Y75_p0951.
eco:b0980.
PATRIC32117183. VBIEscCol129921_1015.

Organism-specific databases

EchoBASEEB0047.
EcoGeneEG10049. appA.

Phylogenomic databases

eggNOGNOG237269.
HOGENOMHOG000118851.
KOK01093.
OMALHNAQFD.
OrthoDBEOG64N9T2.
PhylomeDBP07102.

Enzyme and pathway databases

BioCycEcoCyc:APPA-MONOMER.
ECOL316407:JW0963-MONOMER.
MetaCyc:APPA-MONOMER.

Gene expression databases

GenevestigatorP07102.

Family and domain databases

Gene3D3.40.50.1240. 3 hits.
InterProIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 1 hit.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07102.
PROP07102.

Entry information

Entry namePPA_ECOLI
AccessionPrimary (citable) accession number: P07102
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: August 1, 1991
Last modified: June 11, 2014
This is version 129 of the entry and version 2 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene