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InterPro: IPR001011 Acid phosphatase, class A, bacterial

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UniProtKB

Matches:

157 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR001011 Acid_Pase_classA_bac

Type

Family

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR00483	BACPHPHTASE	157
Signatures in BioMart

InterPro Relationships Help

Parent

IPR000326 Phosphatidic acid phosphatase type 2/haloperoxidase

Children

IPR011158 Nonspecific acid phosphatase, class A

Contains

IPR016118 Phosphatidic acid phosphatase/chloroperoxidase, N-terminal
IPR018296 Acid phosphatase, class A, bacterial, conserved site

GO Term annotation Help

Function

GO:0003993 acid phosphatase activity

Component

GO:0030288 outer membrane-bounded periplasmic space

InterPro annotation

Entry Details in BioMart

Abstract

Class A bacterial acid phosphatases (EC:3.1.3.2) are a group of related proteins that catalyse the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate [1, 2]. This reaction is non-specific and occurs in the periplasm. The enzyme is found as a homotetramer in Morganella morganii (Proteus morganii) [1] and possibly as a homodimer in Salmonella typhimurium, where it is regulated by a 2-component regulatory system formed by the products of the phoP and phoQ genes [2].

Structural links Help

PDB - click here

SCOP: a.111.1.1

CATH: 1.20.144.10

Database links Help

PDBe-motif: PS01157

Enzyme: EC:3.1.3.2

PROSITE doc: PDOC00891

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001011

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P14924 Acid phosphatase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001011	Acid phosphatase, class A, bacterial
IPR018296	Acid phosphatase, class A, bacterial, conserved site
IPR000326	Phosphatidic acid phosphatase type 2/haloperoxidase
IPR016118	Phosphatidic acid phosphatase/chloroperoxidase, N-terminal
IPR011158	Nonspecific acid phosphatase, class A
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Kasahara M, Nakata A, Shinagawa H. Molecular analysis of the Salmonella typhimurium phoN gene, which encodes nonspecific acid phosphatase. J. Bacteriol. 173 6760-5 1991 [PubMed: 1938882] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1938882
2.	Thaller MC, Berlutti F, Schippa S, Lombardi G, Rossolini GM. Characterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii. Microbiology (Reading, Engl.) 140 ( Pt 6) 1341-50 1994 [PubMed: 8081499]

Additional Reading Open in usermanual
	Makde RD, Kumar V, Rao AS, Yadava VS, Mahajan SK. Purification, crystallization and preliminary X-ray diffraction studies of recombinant class A non-specific acid phosphatase of Salmonella typhimurium. Acta Crystallogr. D Biol. Crystallogr. 59 2003 515-8 [PubMed: 12595712] http://dx.doi.org/10.1107/S0907444902022679
	Makde RD, Mahajan SK, Kumar V. Structure and mutational analysis of the PhoN protein of Salmonella typhimurium provide insight into mechanistic details. Biochemistry 46 2007 2079-90 [PubMed: 17263560] http://dx.doi.org/10.1021/bi062180g
	Ishikawa K, Mihara Y, Gondoh K, Suzuki E, Asano Y. X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate. EMBO J. 19 2000 2412-23 [PubMed: 10835340] http://dx.doi.org/10.1093/emboj/19.11.2412
	Makde RD, Dikshit K, Kumar V. Protein engineering of class-A non-specific acid phosphatase (PhoN) of Salmonella typhimurium: modulation of the pH-activity profile. Biomol. Eng. 23 2006 247-51 [PubMed: 16901752] http://dx.doi.org/10.1016/j.bioeng.2006.06.004
	Ishikawa K, Mihara Y, Shimba N, Ohtsu N, Kawasaki H, Suzuki E, Asano Y. Enhancement of nucleoside phosphorylation activity in an acid phosphatase. Protein Eng. 15 2002 539-43 [PubMed: 12200535] http://dx.doi.org/10.1093/protein/15.7.539

InterPro 23.1