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Protein

Periplasmic AppA protein

Gene

appA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381Substrate
Active sitei39 – 391Nucleophile
Binding sitei114 – 1141Substrate
Binding sitei289 – 2891Substrate
Active sitei326 – 3261Proton donor

GO - Molecular functioni

  1. 4-phytase activity Source: EcoCyc
  2. acid phosphatase activity Source: EcoCyc

GO - Biological processi

  1. cellular response to anoxia Source: EcoCyc
  2. cellular response to phosphate starvation Source: EcoCyc
  3. dephosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:APPA-MONOMER.
ECOL316407:JW0963-MONOMER.
MetaCyc:APPA-MONOMER.
BRENDAi3.1.3.26. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic AppA protein
Including the following 2 domains:
Phosphoanhydride phosphohydrolase (EC:3.1.3.2)
Alternative name(s):
pH 2.5 acid phosphatase
Short name:
AP
4-phytase (EC:3.1.3.26)
Gene namesi
Name:appA
Ordered Locus Names:b0980, JW0963
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10049. appA.

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22223 PublicationsAdd
BLAST
Chaini23 – 432410Periplasmic AppA proteinPRO_0000023947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi99 ↔ 130
Disulfide bondi155 ↔ 430
Disulfide bondi200 ↔ 210
Disulfide bondi404 ↔ 413

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP07102.
PRIDEiP07102.

2D gel databases

SWISS-2DPAGEP07102.

Expressioni

Inductioni

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.

Gene expression databases

GenevestigatoriP07102.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP07102. 3 interactions.
STRINGi511145.b0980.

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 3812Combined sources
Helixi49 – 535Combined sources
Helixi71 – 9020Combined sources
Beta strandi96 – 983Combined sources
Turni102 – 1043Combined sources
Beta strandi105 – 1095Combined sources
Helixi113 – 12614Combined sources
Helixi145 – 1473Combined sources
Turni149 – 1535Combined sources
Helixi159 – 16911Combined sources
Turni170 – 1723Combined sources
Helixi174 – 1796Combined sources
Helixi182 – 19211Combined sources
Helixi194 – 1963Combined sources
Helixi198 – 2014Combined sources
Turni204 – 2074Combined sources
Helixi212 – 2154Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi227 – 2293Combined sources
Helixi232 – 24918Combined sources
Helixi254 – 2574Combined sources
Helixi262 – 27918Combined sources
Helixi283 – 2897Combined sources
Helixi291 – 30111Combined sources
Helixi310 – 3123Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi318 – 3247Combined sources
Helixi326 – 33611Combined sources
Beta strandi345 – 3495Combined sources
Beta strandi354 – 3629Combined sources
Turni363 – 3664Combined sources
Beta strandi367 – 37610Combined sources
Helixi379 – 3835Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi395 – 3995Combined sources
Helixi415 – 42511Combined sources
Helixi428 – 4303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP07102.
SMRiP07102. Positions 23-432.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07102.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 465Substrate binding
Regioni325 – 3273Substrate binding

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG237269.
HOGENOMiHOG000118851.
InParanoidiP07102.
KOiK01093.
OMAiLHNAQFD.
OrthoDBiEOG64N9T2.
PhylomeDBiP07102.

Family and domain databases

Gene3Di3.40.50.1240. 3 hits.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07102-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAILIPFLS LLIPLTPQSA FAQSEPELKL ESVVIVSRHG VRAPTKATQL
60 70 80 90 100
MQDVTPDAWP TWPVKLGWLT PRGGELIAYL GHYQRQRLVA DGLLAKKGCP
110 120 130 140 150
QSGQVAIIAD VDERTRKTGE AFAAGLAPDC AITVHTQADT SSPDPLFNPL
160 170 180 190 200
KTGVCQLDNA NVTDAILSRA GGSIADFTGH RQTAFRELER VLNFPQSNLC
210 220 230 240 250
LKREKQDESC SLTQALPSEL KVSADNVSLT GAVSLASMLT EIFLLQQAQG
260 270 280 290 300
MPEPGWGRIT DSHQWNTLLS LHNAQFYLLQ RTPEVARSRA TPLLDLIKTA
310 320 330 340 350
LTPHPPQKQA YGVTLPTSVL FIAGHDTNLA NLGGALELNW TLPGQPDNTP
360 370 380 390 400
PGGELVFERW RRLSDNSQWI QVSLVFQTLQ QMRDKTPLSL NTPPGEVKLT
410 420 430
LAGCEERNAQ GMCSLAGFTQ IVNEARIPAC SL
Length:432
Mass (Da):47,057
Last modified:July 31, 1991 - v2
Checksum:i6510C6C579177F11
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 6616MQDVT…WPVKL → NAGCHPRRMANLAGKT in CAA29031 (PubMed:3038201).CuratedAdd
BLAST
Sequence conflicti75 – 762EL → DV in CAA29031 (PubMed:3038201).Curated
Sequence conflicti112 – 1121D → S in CAA29031 (PubMed:3038201).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB36733.
RefSeqiNP_415500.1. NC_000913.3.
YP_489251.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74065; AAC74065; b0980.
BAA35745; BAA35745; BAA35745.
GeneIDi12930360.
946206.
KEGGiecj:Y75_p0951.
eco:b0980.
PATRICi32117183. VBIEscCol129921_1015.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB36733.
RefSeqiNP_415500.1. NC_000913.3.
YP_489251.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP07102.
SMRiP07102. Positions 23-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07102. 3 interactions.
STRINGi511145.b0980.

2D gel databases

SWISS-2DPAGEP07102.

Proteomic databases

PaxDbiP07102.
PRIDEiP07102.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74065; AAC74065; b0980.
BAA35745; BAA35745; BAA35745.
GeneIDi12930360.
946206.
KEGGiecj:Y75_p0951.
eco:b0980.
PATRICi32117183. VBIEscCol129921_1015.

Organism-specific databases

EchoBASEiEB0047.
EcoGeneiEG10049. appA.

Phylogenomic databases

eggNOGiNOG237269.
HOGENOMiHOG000118851.
InParanoidiP07102.
KOiK01093.
OMAiLHNAQFD.
OrthoDBiEOG64N9T2.
PhylomeDBiP07102.

Enzyme and pathway databases

BioCyciEcoCyc:APPA-MONOMER.
ECOL316407:JW0963-MONOMER.
MetaCyc:APPA-MONOMER.
BRENDAi3.1.3.26. 2026.

Miscellaneous databases

EvolutionaryTraceiP07102.
PROiP07102.

Gene expression databases

GenevestigatoriP07102.

Family and domain databases

Gene3Di3.40.50.1240. 3 hits.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-29.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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(2005) [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(1986) [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(1990) [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(1990)
    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(1992) [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(1999) [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(1991) [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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH INOSITOL HEXAKISPHOSPHATE.

Entry informationi

Entry nameiPPA_ECOLI
AccessioniPrimary (citable) accession number: P07102
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1988
Last sequence update: July 31, 1991
Last modified: March 31, 2015
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.