P07102 (PPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to anoxia Inferred from direct assay PubMed 6282821. Source: EcoCyc cellular response to phosphate starvation Inferred from direct assay PubMed 6282821. Source: EcoCyc
Cellular_component	periplasmic space Inferred from direct assay PubMed 378222. Source: EcoCyc
Molecular_function	4-phytase activity Inferred from direct assay Ref.8. Source: EcoCyc acid phosphatase activity Inferred from direct assay PubMed 6282821. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.1 Ref.7 Ref.8

Chain

23 – 432

410

Periplasmic AppA protein

PRO_0000023947

Regions

Region

42 – 46

5

Substrate binding

Region

325 – 327

3

Substrate binding

Sites

Active site

39

1

Nucleophile

Active site

326

1

Proton donor

Binding site

38

1

Substrate

Binding site

114

1

Substrate

Binding site

289

1

Substrate

Amino acid modifications

Disulfide bond

99 ↔ 130

Disulfide bond

155 ↔ 430

Disulfide bond

200 ↔ 210

Disulfide bond

404 ↔ 413

Experimental info

Sequence conflict

51 – 66

16

MQDVT…WPVKL → NAGCHPRRMANLAGKT in CAA29031. Ref.5

Sequence conflict

75 – 76

2

EL → DV in CAA29031. Ref.5

Sequence conflict

112

1

D → S in CAA29031. Ref.5

Secondary structure

1

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432

Helix Strand Turn

Details...

Beta strand

27 – 38

12

Helix

49 – 53

5

Helix

71 – 90

20

Beta strand

96 – 98

3

Turn

102 – 104

3

Beta strand

105 – 109

5

Helix

113 – 126

14

Helix

145 – 147

3

Turn

149 – 153

5

Helix

159 – 169

11

Turn

170 – 172

3

Helix

174 – 179

6

Helix

182 – 192

11

Helix

194 – 196

3

Helix

198 – 201

4

Turn

204 – 207

4

Helix

212 – 215

4

Beta strand

220 – 222

3

Beta strand

227 – 229

3

Helix

232 – 249

18

Helix

254 – 257

4

Helix

262 – 279

18

Helix

283 – 289

7

Helix

291 – 301

11

Helix

310 – 312

3

Beta strand

314 – 316

3

Beta strand

318 – 324

7

Helix

326 – 336

11

Beta strand

345 – 349

5

Beta strand

354 – 362

9

Turn

363 – 366

4

Beta strand

367 – 376

10

Helix

379 – 383

5

Beta strand

390 – 392

3

Beta strand

395 – 399

5

Helix

415 – 425

11

Helix

428 – 430

3

Sequences

	Sequence		Length	Mass (Da)
	P07102 [UniParc]. Last modified August 1, 1991. Version 2. Checksum: 6510C6C579177F11	FASTA	432	47,057
	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

References

	« Hide 'large scale' referencesShow '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. , 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 277:1453-1474(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.

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.

PIR

B36733.

RefSeq

NP_415500.1. NC_000913.2.
YP_489251.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P07102.

SMR

P07102. Positions 23-432.

ModBase

Search...

Protein-protein interaction databases

IntAct

P07102. 3 interactions.

STRING

511145.b0980.

2D gel databases

SWISS-2DPAGE

P07102.

Proteomic databases

PaxDb

P07102.

PRIDE

P07102.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74065; AAC74065; b0980.
BAA35745; BAA35745; BAA35745.

GeneID

12930360.
946206.

KEGG

ecj:Y75_p0951.
eco:b0980.

PATRIC

32117183. VBIEscCol129921_1015.

Organism-specific databases

EchoBASE

EB0047.

EcoGene

EG10049. appA.

Phylogenomic databases

eggNOG

NOG237269.

HOGENOM

HOG000118851.

KO

K01093.

OMA

SVWANTD.

ProtClustDB

PRK10172.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P07102.

Family and domain databases

InterPro

IPR000560. His_Pase_superF_clade-2.
[Graphical view]

Pfam

PF00328. His_Phos_2. 1 hit.
[Graphical view]

PROSITE

PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07102.

Entry information

Entry name

PPA_ECOLI

Accession

Primary (citable) accession number: P07102

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program