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P07102

- PPA_ECOLI

UniProt

P07102 - PPA_ECOLI

Protein

Periplasmic AppA protein

Gene

appA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (01 Aug 1991)
      Previous versions | rss
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    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

    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

    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.
    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

    MKAILIPFLS LLIPLTPQSA FAQSEPELKL ESVVIVSRHG VRAPTKATQL    50
    MQDVTPDAWP TWPVKLGWLT PRGGELIAYL GHYQRQRLVA DGLLAKKGCP 100
    QSGQVAIIAD VDERTRKTGE AFAAGLAPDC AITVHTQADT SSPDPLFNPL 150
    KTGVCQLDNA NVTDAILSRA GGSIADFTGH RQTAFRELER VLNFPQSNLC 200
    LKREKQDESC SLTQALPSEL KVSADNVSLT GAVSLASMLT EIFLLQQAQG 250
    MPEPGWGRIT DSHQWNTLLS LHNAQFYLLQ RTPEVARSRA TPLLDLIKTA 300
    LTPHPPQKQA YGVTLPTSVL FIAGHDTNLA NLGGALELNW TLPGQPDNTP 350
    PGGELVFERW RRLSDNSQWI QVSLVFQTLQ QMRDKTPLSL NTPPGEVKLT 400
    LAGCEERNAQ GMCSLAGFTQ IVNEARIPAC SL 432
    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.
    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

    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 1, 2014
    This is version 130 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