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Protein

Periplasmic AppA protein

Gene

appA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei38Substrate1
Active sitei39Nucleophile1
Binding sitei114Substrate1
Binding sitei289Substrate1
Active sitei326Proton donor1

GO - Molecular functioni

  • 4-phytase activity Source: UniProtKB-EC
  • acid phosphatase activity Source: UniProtKB-EC
  • inositol phosphate phosphatase activity Source: EcoCyc
  • nucleotidase activity Source: EcoCyc
  • sugar-phosphatase activity Source: EcoCyc

GO - Biological processi

  • cellular response to anoxia Source: EcoCyc
  • cellular response to phosphate starvation Source: EcoCyc
  • dephosphorylation Source: EcoCyc
  • myo-inositol hexakisphosphate dephosphorylation Source: EcoCyc

Keywordsi

Molecular functionHydrolase, Multifunctional enzyme

Enzyme and pathway databases

BioCyciEcoCyc:APPA-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10049 appA

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 223 PublicationsAdd BLAST22
ChainiPRO_000002394723 – 432Periplasmic AppA proteinAdd BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi99 ↔ 130
Disulfide bondi155 ↔ 430
Disulfide bondi200 ↔ 210
Disulfide bondi404 ↔ 413

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP07102
PRIDEiP07102

2D gel databases

SWISS-2DPAGEiP07102

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.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4259354, 22 interactors
IntActiP07102, 3 interactors
STRINGi316385.ECDH10B_1050

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 38Combined sources12
Helixi49 – 53Combined sources5
Beta strandi63 – 65Combined sources3
Helixi71 – 90Combined sources20
Beta strandi96 – 98Combined sources3
Turni102 – 104Combined sources3
Beta strandi105 – 109Combined sources5
Helixi113 – 126Combined sources14
Helixi145 – 147Combined sources3
Turni149 – 153Combined sources5
Helixi159 – 169Combined sources11
Turni170 – 172Combined sources3
Helixi174 – 179Combined sources6
Helixi182 – 192Combined sources11
Helixi194 – 196Combined sources3
Helixi198 – 201Combined sources4
Turni204 – 207Combined sources4
Helixi212 – 215Combined sources4
Beta strandi220 – 222Combined sources3
Beta strandi227 – 229Combined sources3
Helixi232 – 249Combined sources18
Helixi254 – 257Combined sources4
Helixi262 – 279Combined sources18
Helixi283 – 289Combined sources7
Helixi291 – 301Combined sources11
Helixi310 – 312Combined sources3
Beta strandi314 – 316Combined sources3
Beta strandi318 – 324Combined sources7
Helixi326 – 336Combined sources11
Beta strandi345 – 349Combined sources5
Beta strandi354 – 362Combined sources9
Turni363 – 366Combined sources4
Beta strandi367 – 376Combined sources10
Helixi379 – 383Combined sources5
Beta strandi390 – 392Combined sources3
Beta strandi395 – 399Combined sources5
Beta strandi405 – 407Combined sources3
Helixi415 – 425Combined sources11
Helixi428 – 430Combined sources3

3D structure databases

ProteinModelPortaliP07102
SMRiP07102
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07102

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 46Substrate binding5
Regioni325 – 327Substrate binding3

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105D6F Bacteria
ENOG410XRK8 LUCA
HOGENOMiHOG000118851
InParanoidiP07102
KOiK01093
OMAiYVAHDTN
PhylomeDBiP07102

Family and domain databases

CDDicd07061 HP_HAP_like, 1 hit
Gene3Di3.40.50.1240, 3 hits
InterProiView protein in InterPro
IPR033379 Acid_Pase_AS
IPR000560 His_Pase_clade-2
IPR029033 His_PPase_superfam
PfamiView protein in Pfam
PF00328 His_Phos_2, 1 hit
SUPFAMiSSF53254 SSF53254, 1 hit
PROSITEiView protein in PROSITE
PS00616 HIS_ACID_PHOSPHAT_1, 1 hit
PS00778 HIS_ACID_PHOSPHAT_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti51 – 66MQDVT…WPVKL → NAGCHPRRMANLAGKT in CAA29031 (PubMed:3038201).CuratedAdd BLAST16
Sequence conflicti75 – 76EL → DV in CAA29031 (PubMed:3038201).Curated2
Sequence conflicti112D → S in CAA29031 (PubMed:3038201).Curated1

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
WP_001300464.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74065; AAC74065; b0980
BAA35745; BAA35745; BAA35745
GeneIDi946206
KEGGiecj:JW0963
eco:b0980
PATRICifig|1411691.4.peg.1293

Similar proteinsi

Entry informationi

Entry nameiPPA_ECOLI
AccessioniPrimary (citable) accession number: P07102
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: August 1, 1991
Last modified: March 28, 2018
This is version 154 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

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