Reviewed, UniProtKB/Swiss-Prot P07102 (PPA_ECOLI)

Names and origin

Protein names

Recommended name:
    Periplasmic appA protein
Including the following 2 domains:
    1- Recommended name:
            Phosphoanhydride phosphohydrolase
              EC=3.1.3.2
        Alternative name(s):
            pH 2.5 acid phosphatase
              Short name=AP
    2- Recommended name:
            4-phytase
              EC=3.1.3.26

Gene names

Name:	appA
Ordered Locus Names:	b0980, JW0963

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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
Gene Ontology (GO)
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4-phytase activity Inferred from electronic annotation. Source: EC acid phosphatase activity Inferred from electronic annotation. Source: EC
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

Sites

Active site

39

1

Nucleophile

Active site

326

1

Proton donor

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

28 – 38

11

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

Helix

174 – 179

6

Helix

182 – 192

11

Helix

194 – 196

3

Helix

198 – 201

4

Helix

212 – 215

4

Beta strand

220 – 223

4

Beta strand

226 – 229

4

Helix

231 – 249

19

Helix

254 – 257

4

Helix

262 – 279

18

Helix

283 – 301

19

Helix

310 – 312

3

Beta strand

314 – 316

3

Beta strand

318 – 324

7

Helix

326 – 336

11

Beta strand

354 – 362

9

Turn

363 – 365

3

Beta strand

368 – 376

9

Helix

379 – 383

5

Beta strand

390 – 392

3

Beta strand

395 – 398

4

Helix

415 – 425

11

Helix

428 – 430

3

Sequences

	Sequence		Length	Mass (Da)
	P07102-1 [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: 2168385] [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: 8905232] [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: 9278503] [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: 16738553] [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: 3038201] [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: 1658595] [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: 8387749] [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: 10696472] [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: 1429631] [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: 10655611] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

AP_001609.1.
NP_415500.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

2-D gel databases

SWISS-2DPAGE

P07102.

Genome annotation databases

GeneID

946206.

GenomeReviews

Gene locus JW0963 in contig AP009048_GR.
Gene locus b0980 in contig U00096_GR.

KEGG

ecj:JW0963.
eco:b0980.

Organism-specific databases

EchoBASE

EB0047.

EcoGene

EG10049. appA.

CMR

Search...

Phylogenomic databases

HOGENOM

P07102.

OMA

P07102. CLNREKQ.

Enzyme and pathway databases

BioCyc

EcoCyc:APPA-MON.
MetaCyc:APPA-MON.

Family and domain databases

InterPro

IPR000560. Histidine_acid_Pase.
[Graphical view]

Pfam

PF00328. Acid_phosphat_A. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

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:	June 16, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)