Class B acid phosphatase precursor - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0AE22 (APHA_ECOLI)

Last modified November 3, 2009. Version 47. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Class B acid phosphatase
EC=3.1.3.2

Gene names

Name:	aphA
Synonyms:	napA, yjbP
Ordered Locus Names:	b4055, JW4015

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	237 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Dephosphorylates several organic phosphomonoesters and catalyzes the transfer of low-energy phosphate groups from phosphomonoesters to hydroxyl groups of various organic compounds. Preferentially acts on aryl phosphoesters. Might function as a broad-spectrum dephosphorylating enzyme able to scavenge both 3'- and 5'-nucleotides and also additional organic phosphomonoesters.
Catalytic activity	A phosphate monoester + H₂O = an alcohol + phosphate.
Cofactor	Binds 1 magnesium ion per subunit.
Enzyme regulation	Activated by magnesium and ethanol. Inhibited by EDTA, nucleosides, inorganic phosphate and calcium.
Subunit structure	Homotetramer.
Subcellular location	Periplasm Potential.
Sequence similarities	Belongs to the class B bacterial acid phosphatase family.
Biophysicochemical properties	pH dependence: Optimum pH is 6-6.5 with 5'-AMP as substrate, and pH 5.5-6 with 3'-AMP or pNPP as substrate.

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Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro
Molecular function	acid phosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
yeeL	P76349	1	EBI-549463,EBI-1126699

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

Or 23 Ref.6

Chain

26 – 237

212

Class B acid phosphatase

PRO_0000024004

Sites

Metal binding

Magnesium

Metal binding

Magnesium; via carbonyl oxygen

Metal binding

192

Magnesium

Secondary structure

237

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0AE22-1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 35C1BFE6DF9E530D
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FASTA

237

26,104

        10         20         30         40         50         60 
MRKITQAISA VCLLFALNSS AVALASSPSP LNPGTNVARL AEQAPIHWVS VAQIENSLAG 

        70         80         90        100        110        120 
RPPMAVGFDI DDTVLFSSPG FWRGKKTFSP ESEDYLKNPV FWEKMNNGWD EFSIPKEVAR 

       130        140        150        160        170        180 
QLIDMHVRRG DAIFFVTGRS PTKTETVSKT LADNFHIPAT NMNPVIFAGD KPGQNTKSQW 

       190        200        210        220        230 
LQDKNIRIFY GDSDNDITAA RDVGARGIRI LRASNSTYKP LPQAGAFGEE VIVNSEY

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Marquez S.M., Gumport R.I. Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product." Thaller M.C., Schippa S., Bonci A., Cresti S., Rossolini G.M. FEMS Microbiol. Lett. 146:191-198(1997) [PubMed: 9011040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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], SEQUENCE REVISION. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-37. Strain: K12 / EMG2.
[7]	"The first structure of a bacterial class B acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold." Calderone V., Forleo C., Benvenuti M., Cristina Thaller M., Maria Rossolini G., Mangani S. J. Mol. Biol. 335:761-773(2004) [PubMed: 14687572] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 26-237.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

U51210 Genomic DNA. Translation: AAA96322.1.
X86971 Genomic DNA. Translation: CAA60534.1.
U00006 Genomic DNA. Translation: AAC43149.1. Frameshift.
U00096 Genomic DNA. Translation: AAC77025.1.
AP009048 Genomic DNA. Translation: BAE78057.1.

PIR

S54790.

RefSeq

AP_004556.1.
NP_418479.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N8N	X-ray	1.69	A	26-237	[»]
1N9K	X-ray	2.20	A/B	26-237	[»]
1RMQ	X-ray	2.00	A/B	26-237	[»]
1RMT	X-ray	1.40	A/B/C/D	26-237	[»]
1RMY	X-ray	1.75	A/B	26-237	[»]
2B82	X-ray	1.25	A/B	27-237	[»]
2B8J	X-ray	2.03	A/B	27-237	[»]
2G1A	X-ray	2.00	A/B	26-237	[»]
2HEG	X-ray	1.50	A/B	27-237	[»]
2HF7	X-ray	1.60	A/B	27-237	[»]
3CZ4	X-ray	1.70	A	26-237	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AE22. 1 interaction.

STRING

P0AE22.

Genome annotation databases

GeneID

948562.

GenomeReviews

Gene locus JW4015 in contig AP009048_GR.
Gene locus b4055 in contig U00096_GR.

KEGG

ecj:JW4015.
eco:b4055.

Organism-specific databases

EchoBASE

EB1878.

EcoGene

EG11934. aphA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AE22.

OMA

GQNTKTQ.

Enzyme and pathway databases

BioCyc

EcoCyc:APHA-MON.
MetaCyc:APHA-MON.

BRENDA

3.1.3.2. 246.

Gene expression databases

Genevestigator

P0AE22.

Family and domain databases

InterPro

IPR005519. Acid_phosphat_B.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view]

Pfam

PF03767. Acid_phosphat_B. 1 hit.
[Graphical view]

PIRSF

PIRSF017818. Acid_Ptase_B. 1 hit.

TIGRFAMs

TIGR01672. AphA. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

APHA_ECOLI

Accession

Primary (citable) accession number: P0AE22
Secondary accession number(s): P32697

Q57085

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	November 3, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents