APHA_SALTY
ID APHA_SALTY Reviewed; 237 AA.
AC P58683;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Class B acid phosphatase;
DE Short=CBAP;
DE EC=3.1.3.2 {ECO:0000269|PubMed:3049613, ECO:0000269|PubMed:6256351};
DE AltName: Full=Non-specific acid phosphatase II;
DE Flags: Precursor;
GN Name=aphA; OrderedLocusNames=STM4249;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=6256351; DOI=10.1016/s0021-9258(19)70147-1;
RA Uerkvitz W., Beck C.F.;
RT "Periplasmic phosphatases in Salmonella typhimurium LT2. A biochemical,
RT physiological, and partial genetic analysis of three nucleoside
RT monophosphate dephosphorylating enzymes.";
RL J. Biol. Chem. 256:382-389(1981).
RN [3]
RP FUNCTION AS A PHOSPHOTRANSFERASE, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, AND CRYSTALLIZATION.
RC STRAIN=LT2;
RX PubMed=3049613; DOI=10.1016/s0021-9258(19)37662-8;
RA Uerkvitz W.;
RT "Periplasmic nonspecific acid phosphatase II from Salmonella typhimurium
RT LT2. Crystallization, detergent reactivation, and phosphotransferase
RT activity.";
RL J. Biol. Chem. 263:15823-15830(1988).
CC -!- FUNCTION: Dephosphorylates several organic phosphate monoesters such as
CC 3'-UMP, 5'-UMP and pNPP (PubMed:6256351). Also has a phosphotransferase
CC activity catalyzing the transfer of low-energy phosphate groups from
CC organic phosphate monoesters to free hydroxyl groups of various organic
CC compounds such as the 2'-, 3-, or 5'-hydroxyls of nucleosides and
CC nucleotides (PubMed:3049613). Also displays significant phosphomutase
CC activity since it is able to catalyze the transfer of the phosphate
CC group of 3'-AMP from the 3'-position both to the 2'- and 5'-positions.
CC One of the physiological functions of the phosphohydrolytic activity of
CC the enzyme is believed to be the scavenging of organic phosphate esters
CC that otherwise cannot pass the cytoplasmic membrane (PubMed:6256351).
CC {ECO:0000269|PubMed:3049613, ECO:0000269|PubMed:6256351}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000269|PubMed:3049613, ECO:0000269|PubMed:6256351};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q540U1};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q540U1};
CC -!- ACTIVITY REGULATION: Nucleosides, and particularly 2'-
CC deoxyribonucleosides, are potent inhibitors of the phosphatase
CC activity. The phosphatase activity is also inhibited by inorganic
CC phosphate and EDTA in vitro. {ECO:0000269|PubMed:3049613,
CC ECO:0000269|PubMed:6256351}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.30 mM for 5'-UMP (at 37 degrees Celsius and pH 6.5)
CC {ECO:0000269|PubMed:6256351};
CC pH dependence:
CC Optimum pH is 5.0-5.5 and 6.5 for the phosphatase activity with 3'-
CC UMP and 5'-UMP as substrate, respectively.
CC {ECO:0000269|PubMed:6256351};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:3049613}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:6256351}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a severely decreased
CC growth rate on 5'-UMP as pyrimidine source.
CC {ECO:0000269|PubMed:6256351}.
CC -!- SIMILARITY: Belongs to the class B bacterial acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL23073.1; -; Genomic_DNA.
DR RefSeq; NP_463114.1; NC_003197.2.
DR RefSeq; WP_000724435.1; NC_003197.2.
DR AlphaFoldDB; P58683; -.
DR SMR; P58683; -.
DR STRING; 99287.STM4249; -.
DR PaxDb; P58683; -.
DR EnsemblBacteria; AAL23073; AAL23073; STM4249.
DR GeneID; 1255775; -.
DR KEGG; stm:STM4249; -.
DR PATRIC; fig|99287.12.peg.4469; -.
DR HOGENOM; CLU_081496_0_0_6; -.
DR OMA; PEFWEKM; -.
DR PhylomeDB; P58683; -.
DR BioCyc; SENT99287:STM4249-MON; -.
DR SABIO-RK; P58683; -.
DR EvolutionaryTrace; P58683; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07499; HAD_CBAP; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR005519; Acid_phosphat_B-like.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR010025; HAD-SF_ppase_IIIB_AphA.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF03767; Acid_phosphat_B; 1.
DR PIRSF; PIRSF017818; Acid_Ptase_B; 1.
DR SFLD; SFLDG01127; C1.3:_Acid_Phosphatase_Like; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01672; AphA; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..237
FT /note="Class B acid phosphatase"
FT /id="PRO_0000024009"
FT ACT_SITE 69
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
FT ACT_SITE 71
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
FT BINDING 137..138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
SQ SEQUENCE 237 AA; 26315 MW; 386E11DC84C16269 CRC64;
MKKITLALSA VCLLFTLNHS ANALVSSPST LNPGTNVAKL AEQAPVHWVS VAQIENSLTG
RPPMAVGFDI DDTVLFSSPG FWRGKKTYSP DSDDYLKNPA FWEKMNNGWD EFSIPKEVAR
QLIDMHVRRG DSIYFVTGRS QTKTETVSKT LADNFHIPAA NMNPVIFAGD KPEQNTKVQW
LQEKNMRIFY GDSDNDITAA RDCGIRGIRI LRAANSTYKP LPQAGAFGEE VIVNSEY
