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P07102

- PPA_ECOLI

UniProt

P07102 - PPA_ECOLI

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Protein

Periplasmic AppA protein

Gene

appA

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.

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: Chromosome, UP000000625: 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 – 3812
Helixi49 – 535
Helixi71 – 9020
Beta strandi96 – 983
Turni102 – 1043
Beta strandi105 – 1095
Helixi113 – 12614
Helixi145 – 1473
Turni149 – 1535
Helixi159 – 16911
Turni170 – 1723
Helixi174 – 1796
Helixi182 – 19211
Helixi194 – 1963
Helixi198 – 2014
Turni204 – 2074
Helixi212 – 2154
Beta strandi220 – 2223
Beta strandi227 – 2293
Helixi232 – 24918
Helixi254 – 2574
Helixi262 – 27918
Helixi283 – 2897
Helixi291 – 30111
Helixi310 – 3123
Beta strandi314 – 3163
Beta strandi318 – 3247
Helixi326 – 33611
Beta strandi345 – 3495
Beta strandi354 – 3629
Turni363 – 3664
Beta strandi367 – 37610
Helixi379 – 3835
Beta strandi390 – 3923
Beta strandi395 – 3995
Helixi415 – 42511
Helixi428 – 4303

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:August 1, 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi B36733.
RefSeqi NP_415500.1. NC_000913.3.
YP_489251.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DKL X-ray 2.30 A/B 23-432 [» ]
1DKM X-ray 2.25 A 23-432 [» ]
1DKN X-ray 2.40 A 23-432 [» ]
1DKO X-ray 2.38 A 23-432 [» ]
1DKP X-ray 2.28 A 23-432 [» ]
1DKQ X-ray 2.05 A 23-432 [» ]
ProteinModelPortali P07102.
SMRi P07102. Positions 23-432.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P07102. 3 interactions.
STRINGi 511145.b0980.

2D gel databases

SWISS-2DPAGE P07102.

Proteomic databases

PaxDbi P07102.
PRIDEi P07102.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74065 ; AAC74065 ; b0980 .
BAA35745 ; BAA35745 ; BAA35745 .
GeneIDi 12930360.
946206.
KEGGi ecj:Y75_p0951.
eco:b0980.
PATRICi 32117183. VBIEscCol129921_1015.

Organism-specific databases

EchoBASEi EB0047.
EcoGenei EG10049. appA.

Phylogenomic databases

eggNOGi NOG237269.
HOGENOMi HOG000118851.
InParanoidi P07102.
KOi K01093.
OMAi LHNAQFD.
OrthoDBi EOG64N9T2.
PhylomeDBi P07102.

Enzyme and pathway databases

BioCyci EcoCyc:APPA-MONOMER.
ECOL316407:JW0963-MONOMER.
MetaCyc:APPA-MONOMER.

Miscellaneous databases

EvolutionaryTracei P07102.
PROi P07102.

Gene expression databases

Genevestigatori P07102.

Family and domain databases

Gene3Di 3.40.50.1240. 3 hits.
InterProi IPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view ]
Pfami PF00328. His_Phos_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 1 hit.
PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1990) [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(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.

Entry informationi

Entry nameiPPA_ECOLI
AccessioniPrimary (citable) accession number: P07102
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: August 1, 1991
Last modified: October 29, 2014
This is version 131 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