P58683 (APHA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Class B acid phosphatase
Short name=CBAP
EC=3.1.3.2

Alternative name(s):
Non-specific acid phosphatase II

Gene names

Name:	aphA
Ordered Locus Names:	STM4249

Organism

Salmonella typhimurium

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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

General annotation (Comments)

Function	Dephosphorylates several organic phosphate monoesters such as 3'-UMP, 5'-UMP and pNPP. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds such as the 2'-, 3-, or 5'-hydroxyls of nucleosides and nucleotides. Also displays significant phosphomutase activity since it is able to catalyze the transfer of the phosphate group of 3'-AMP from the 3'-position both to the 2'- and 5'-positions. One of the physiological functions of the phosphohydrolytic activity of the enzyme is believed to be the scavenging of organic phosphate esters that otherwise cannot pass the cytoplasmic membrane. Ref.2 Ref.3
Catalytic activity	A phosphate monoester + H2O = an alcohol + phosphate. Ref.2 Ref.3
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Enzyme regulation	Nucleosides, and particularly 2'-deoxyribonucleosides, are potent inhibitors of the phosphatase activity. The phosphatase activity is also inhibited by inorganic phosphate and EDTA in vitro. Ref.2 Ref.3
Subunit structure	Homotetramer. Ref.3
Subcellular location	Periplasm Ref.2.
Disruption phenotype	Cells lacking this gene show a severely decreased growth rate on 5'-UMP as pyrimidine source. Ref.2
Sequence similarities	Belongs to the class B bacterial acid phosphatase family.
Biophysicochemical properties	Kinetic parameters: KM=0.30 mM for 5'-UMP (at 37 degrees Celsius and pH 6.5) pH dependence: Optimum pH is 5.0-5.5 and 6.5 for the phosphatase activity with 3'-UMP and 5'-UMP as substrate, respectively.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 237	214	Class B acid phosphatase		PRO_0000024009
Regions
	Region	137 – 138	2	Substrate binding By similarity
Sites
	Active site	69	1	Nucleophile By similarity
	Active site	71	1	Proton donor By similarity
	Metal binding	69	1	Magnesium By similarity
	Metal binding	71	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	192	1	Magnesium By similarity
	Binding site	177	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P58683 [UniParc]. Last modified January 31, 2002. Version 1. Checksum: 386E11DC84C16269	FASTA	237	26,315
	10 20 30 40 50 60 MKKITLALSA VCLLFTLNHS ANALVSSPST LNPGTNVAKL AEQAPVHWVS VAQIENSLTG 70 80 90 100 110 120 RPPMAVGFDI DDTVLFSSPG FWRGKKTYSP DSDDYLKNPA FWEKMNNGWD EFSIPKEVAR 130 140 150 160 170 180 QLIDMHVRRG DSIYFVTGRS QTKTETVSKT LADNFHIPAA NMNPVIFAGD KPEQNTKVQW 190 200 210 220 230 LQEKNMRIFY GDSDNDITAA RDCGIRGIRI LRAANSTYKP LPQAGAFGEE VIVNSEY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[2]	"Periplasmic phosphatases in Salmonella typhimurium LT2. A biochemical, physiological, and partial genetic analysis of three nucleoside monophosphate dephosphorylating enzymes." Uerkvitz W., Beck C.F. J. Biol. Chem. 256:382-389(1981) [PubMed: 6256351] [Abstract] Cited for: FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. Strain: LT2.
[3]	"Periplasmic nonspecific acid phosphatase II from Salmonella typhimurium LT2. Crystallization, detergent reactivation, and phosphotransferase activity." Uerkvitz W. J. Biol. Chem. 263:15823-15830(1988) [PubMed: 3049613] [Abstract] Cited for: FUNCTION AS A PHOSPHOTRANSFERASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, CRYSTALLIZATION. Strain: LT2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006468 Genomic DNA. Translation: AAL23073.1.
RefSeq	NP_463114.1. NC_003197.1.
3D structure databases
ProteinModelPortal	P58683.
SMR	P58683. Positions 27-237.
ModBase	Search...
Proteomic databases
PRIDE	P58683.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1255775.
GenomeReviews	Gene locus STM4249 in contig AE006468_GR.
KEGG	stm:STM4249.
PATRIC	32387403. VBISalEnt20916_4469.
Phylogenomic databases
HOGENOM	HBG698065.
OMA	GQNTKTQ.
ProtClustDB	PRK11009.
Enzyme and pathway databases
BioCyc	STYP99287:STM4249-MONOMER.
Family and domain databases
InterPro	IPR005519. Acid_phosphat_B. IPR023214. HAD-like_dom. IPR010025. HAD-SF_ppase_IIIB_AphA. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KO	K03788.
Pfam	PF03767. Acid_phosphat_B. 1 hit. [Graphical view]
PIRSF	PIRSF017818. Acid_Ptase_B. 1 hit.
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01672. AphA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

APHA_SALTY

Accession

Primary (citable) accession number: P58683

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	January 31, 2002
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program