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   27-MAR-2024, entry version 123.
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; Pseudomonadota; 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=0.3 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
CC         3'-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; 99287-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-MONOMER; -.
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; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01672; AphA; 1.
DR   Pfam; PF03767; Acid_phosphat_B; 1.
DR   PIRSF; PIRSF017818; Acid_Ptase_B; 1.
DR   SFLD; SFLDG01127; C1.3:_Acid_Phosphatase_Like; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 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
//